Обнаружение и изучение физикохимических свойств протеолитических ферментов гриба Eremothecum Ashbyii
Rossman T., Norris G., and Troll W.-Inhibition of macromolecu-lar synthesis in Echerichia coli by protease inhibitors. Specific reversal by glutathion of the effects of chloromethyl ketones. J. Biol .Chem., 1974, v. 249, p. 3412−3417. Gripon J.C., Rhee S.H., and Hofmann T.-N-terminal amino acid sequeces of acid proteases fromPenicillium roqueforti and Rhi-zopus chinensis and alignment with… Читать ещё >
Обнаружение и изучение физикохимических свойств протеолитических ферментов гриба Eremothecum Ashbyii (реферат, курсовая, диплом, контрольная)
Содержание
- — 139 -6. ВЫВОДЫ
1. Впервые изучена протеолитическая система флавиногенного гриба E.-ashbyii. Показано существование четырех оптимумов протеолитической активности. в экстрактах из мицелия гриба при рН 4,0- 7,5- 9*5 и Щ5. В &bdquo-культуральной жидкости, обнаружена протеолитическая активность с оптимумами рН 4,0 и 7,5.
2. Изучено изменение активности обнаруженных протеиназ в процессе роста гриба. Установлено, что активность этих ферментов по-разному изменяется в процессе развития культуры. Наиболее высокая активность кислой. и нейтральной протеиназ отмечена в 48-часовом мицелии, а активность. щелочных протеиназ — в 120-часовом мицелии. Уровень активности кислой протеиназы в культуральной жидкости не изменялся в процессе культивирования гриба, а активности нейтральной и щелочных, протеиназ в среде были наиболее высокими в 120-часовой культуре.
— 3. Показано, что. при использ.о.вании. казеина. в, качестве. единственного, источника.азота.происходит.индукция.биосинтеза протеиназ с оптимумами. рН 4,0. и. 7,3. Прибавление. ионов аммония, ингибирует оинтез этих ферментов, что. свидетельствует об участии механизма азотной катаболитной репрессии. в регуляции.их образования. Ингибитор. транскрипции. 8-оксихинолин предотвращает индукцию кислой протеиназы казеином.
4. Разработана процедура очистки комплекса внутриклеточных нейтральных протеиназ/ включающая фракционирование, белков сульфатом, аммония, их температурную обработку, хроматографию на сефадексе G-75 и ионообменную хроматографию на ДЭАЭ-целлюлозе, в результате чего были выделены три фермента мицелия гриба е. ash.
— 120 -byii «протеиназы E, F и G.
5. Ингибитор сериновых протеиназ фенилметилсульфонилфторид о
С ФМСФ) в концентрации, а также п- Хлормеркуробензоат
С п-ХМБ) в концентрации Ю^М угнетают активность протеиназ Е, Р и s. ЭДТА в концентрации 10"*% не влияет на активность протеиназы Е, активирует протеиназу F и ингибирует протеиназу ff. б. Получен выоокоочищенный препарат оериновой протеиназы Е. Определены свойства этого фермента. Оптимум рН находится в пределах 6,0 -8,5 без четко выраженного максимума,.Наиболее высокую активность протеиназа Е обнаруживает. при 60°* Фермент относительно стабилен в. интервале рН 6,0 — 9,0 (в .течение 24 ч при. комнатной температуре сохраняет более 50 $ от исходной активности). Из исследованных белковых, оубстратов С казеин,' гемоглобин, азо-казеин- азоальбумин, .альбумин сыворотки крови человека, бычий, сывороточный. альбумин) .протеиназа. Е наиболее эффективно гидро-лизует.азоказеин. .Фермент, не расщепляет -бензоил-. i — арги-н.ин-п-нитроанилид, — следовательно он лишен амидазной. активности. Однако, протеиназа. Е. расщепляет-N — бензоил-аргинин метиловый эфир, выявляя эстеразную активность. .Фермент полностью ингибируетоя. ионами. не44- иСдд14* в концентрации. 10"*%. Ионы .,. Ms4″,
Са"14″, Со"14″ и Zn"1"1″."активируют.протеиназу. Е. Особенно сильное. активирование наблюдается в присутствии. ионов Mg"1"1″ С больше, чем в. Л раза). Молекулярная масса. протеиназы Е определена методом гель-фильтрации на сефадексе G-75 и составляет 51 000 Да.
7. &bdquo-Выявлен и. частично, очищен при. помощи гель-фильтрации, на сефадексе G-7.5 термостабильный, внутриклеточный ингибитор протеиназы Е- по-видимому, белковой природы. Препарат ингибитора угнетал активность протеиназы Е, а также трипсина при рН 7,5-
8. Впервые обнаружена полная инактивация ферментов флавиногене за ГТР-циклогидролазы и рибофлавинкиназы дрожжей Picbia gra.1-liermondii при инкубации этих ферментов in vitro с протеиназой Е.
1.Kolzer H., Betz H. and Ebner E.-Intracellular proteinases in microorganisms • Curr. (Гор.Cell. Regul., 3975"v.9"P" ID3-I46. fi. Sw±fez€srtR"Ii"-The inactivation of: microbial enzymes in vivo. An-mu Rev, Microbiol.*39 771*. 3I*p. 135−157.
2. Ъ Андеркофлер A, В кн.: Производство, и применение ферментных препаратов в пищевой промышленности. М.: Пищепромиздат, 1963, с. 48.
3. Бабакина. В/Г/ гПрименение ферментов в производстве кожи. Мл Ростехиздат, 1962.. ?• Диканская З. М, Образование рибофлавина микроскопическим грибом, Eremotheciumi ashbyii. — Тр. Ин-та микробиологии, 1954,3.
4. Hartley В.С. -Proteolytic enzymes. Annu. Rev"Biochem.-«i960, v"29 «ръ45−72.
5. Kovaleva"G.G. .Shimanskaya M-P. and Stepanov WM.-The site of diazoacetil inhibitor attachment to acid proteinase of Aspergillus awamorl-an analog of penicillopepsin and pepsin. Biochee* Biopbys.Hes.Commmi., 1972, v. A9 tp. Io75-I03l.
6. ХО. Ь1игСЛ>. «and Hatano H.-An asparfcic acid residue at the active site of Rhodotorula gltrfcinus acid protease. FEBS Lett», 1974;, v.42"p* 352−354.
7. Arch.Micrabiol., 1980, v"32^, p*269−274.
8. TsuJita T. t and Endo A.—iDitr acellular localization of two mo-lecnl ar forms of membrane acid protease in Aspergilltts oryzae* J*. Biochem^/Iobyo/, l980, v"88,p.H3-I20.
9. Tapia G."Curotto E., O’Reilly В", and Gonzales G"-Izolation and partial characterization of an extracellular protease from Spo-TOtricham dimorphocportm^FEBS Lett, ,!98Ifv"I30tpw:" 205 -207.
10. Rickert W"S", and McBride P. A.-Structural and functional determinants of Mucor miehei protease. IH^Is olation and composition, of the carbohydrate moiety•.Biochim. Biophys. Act a", 197^, v.336,p* 437−444,.
11. Murao S*., Morita H*, ramamoto X., and Oda K.-Partial structure of glycopeptide obtained from Scytalidium lignicolim acid protease A"Agric".Biol"Chem", 378"v"42, p"3343—1349″.
12. Tsujita T", and Endo A"-Chemical properties of the polysaccha-idea associated with, acid protease of Aspergillus oryzae grown onsolid bran media. J. Biochem"/Tokyo/, 1977, v"8X, p. 1063−1070.
13. Haumard JV, and Raymond М. ГГ"-Further characterization of the Penicillium: roqueforti acid protease. Biochimie, I979*v"6I, p. :979−982.
14. Martin P", Raymond H. K", Bricas E., ahd Ribadeau Dumas B.-Kinetic studies of the action of Mucor pusillas, Mucor miehei acid proteases chymosins A and В on a synthetic chromopfaocric hexapeptide. Biochinu Biophys.Acta., I980, v.6l2, pw4I0−420.
15. Hwang J.,"and Hseu Т.Н.-Specificity of the acid protease from Monascus kaoliang towards the ftchain of oxidized insulin. Bioc-im. Biophys-Acta, 1980, v. 614, p. &607−6I2 .
16. Kimura Mayumi, Takeuchi M., Hayashi K^, andl Xchishima E.-Substrate specificity of carboxyl proteinase of Aspergillus so-5ae.Cxarr.Mcrobiol", 3979"v"3, p. 153—156.
17. Lenoir J., Auberger B., and Gripon J.C.-Les caracteres du sis-temeproteoOLytique de Penicillium caseieolxm. Ill. Caracterization &-гтше protease acide. bait, 1979* v.59 244−268.
18. Robinson ГГ.С., Neurath H., and Walsh K. A.-Preparation and characterization. of guani&inated trypsinogen. and? -guarttd inated trypsin. Biochemistry, 1973* v. 32, pv4I4−420.
19. Davidson R., Gertler A."an& Hofmann T.-Aspergillus oryzae acid proteinase. Pacification and properties, and formation of 7T"chy-motrypsiru Biochem. J., 1975I47"P. 45−53.
20. Sharma S.K.rand Hopkins T.R.-Activation of bovine chymotrypsinogen A. Isolation. ¦ and characterization of Jul and OJchymotryp-sin. Biochemistry, 1979, v. I8, p. I008-I0I3.
21. Gripon J.C., Rhee S.H., and Hofmann T.-N-terminal amino acid sequeces of acid proteases fromPenicillium roqueforti and Rhi-zopus chinensis and alignment with penicillopepsin and mammalian proteases. Can. JVBiochem., 1977*v"55"p. 504−506.
22. Tickle I.J., and Bluhndell T.L.-Homology among acid proteases: оcomparison of crystal structures at 3 A resolution of acid proteases from Rhizopus chinensis and Endotbia p arasitica. Proc. Natl. Acad.Sci.IT.S.A., 1977, v.74,p. 556−559.
23. Tang J., James M.N.G., Hsu I.N., Jenkins J.A., and Blundell T.L.-Structural evidence for gen duplication, in theevolution of the acid proteases. Nature /London/, 1978, v.271,p.618−621.
24. Tang J.-Evolution in the structure and function of carboxyl proteases. Mol. Cell. Biochem., I$ 79 26, p. 93—109.
25. Isolation. Amino acid sequences of tryptic peptides.Bioorg.Khim.1.8Q, v.6,p. 1765−1777.
26. Cohen В.L.-Transport and trtiT ization of proteins by fungi, 1980, p.411−430. In J.V. Payne /ed. /. Microorganisms and nitrogen sources. John Wiley&Sons Ltd. Chichester.
27. Matsushima K., Hayakawa M., Ito M.^amd Whimada K.-Features of the proteolytic enzyme system of hyperacid productive and non-acid — productive fungi. J.Gen. Appl.Microbiol., T98I"v.27,p.423 -426.
28. J. Bacterid., 1974, v. 117, p. 1035−1042.
29. Govind. N.S., Merta. B. «Charma M., and Modi V.V.-Protease and ca-rcrtenogenesis in B1 akeslea trispora. Phytochem., I98I, v. II, p.24 832 485.
30. Jonsson A. G"-Purification and some properties of a. protease from Alternaria tenuissimia.Arch.Biochem.Biophys., l969, v. 129, p.62.67.
31. Tomoda K. rMiJita K.*Maepima К" .Дакашпга M., Ktmo M., and Isono M.-Production, purification and general properties of fusariuro alkaline protease. JVTakeda ResLab. ,-l979,v. 38, p. 33−43.
32. Ebeling W., Hennrich N., KLockov M., Me.tzH., Qrth H.3V"and bang H.-Proteinase К fro® Eritiracbium album Limber. Eur. J. Biochem., 19 74, v. 47 «p. 91−97.
33. Kominami E., HoffschuLte H., Leuschel L-, Maier K., andHolzer H.-{Ehee substrate specificity of proteinase В from baker 's yeast. Biochim. Biophys. Acta, I981rv"661 «p. 136−141.
34. Lindberg R.A., Eirich L.D., Price J.S.r?olfinbarger L., and Druc-ker H.-Alkaline protease from Neurospora crass a. Purification and partial ciharacteriz: ation. J. Biol. Chem., l98I, v.256"p. 8II-8I4.
35. Martin. S.H., Johnson A.G.-An extracellular protease from Aspergillus ftimigatus. Can. J. Bioxxhem.^l965rv. 43, p. 1745−1753.
36. Шатаева. Л^К., Орлиевская O. Bv, Лишковокая Г/В^, Самсонов Т-В. ~ Энзиматическая активность террилитина. Биохимия, 1973, т.: 38, с. 1169 1174.
37. Nordwig A., Bretschneider G.-Nonspecific colagenolytic activi-vity.Дус1г olysisof native colagen by a. mold protease. Biochim. Biophys .Acta, 3971″ v. 250, p.408−415.
38. Gertler A., ffayashi K.-Esterolytic, elastase-1 ike activity of purified alkaline proteinase from Aspergillus so^ae. Biochim. Biophys. Act a, 1971″ v. 235 «P. 378−380.
39. Morihara K., Oka T."Tsuzuki H"-Comparative study of various serine alkaline proteinases from microorganisms. Esterase activity against N-acylated peptide ester substrates.Arch. Biochem. Biophys ., 1974"v.165,p.72−79.
40. Turkova J., Mikes O. -Specificity of alkaline proteinase of.
41. Aspergillus flavus • Biochim. Biophys. Acta, 1970, v. I98, p. 386−388,.
42. Ушакова В.И.у Далько.Л.'Е., Егоров Н-С.-Изучение протеазного комплекса, синтезируемого A.kanagawaensis., в. связи с его. фибринолитической активностью*-Биол.науки, 1974, т. 17, с. 93 97.
43. Morihara К., Oka Т., Tsuzuki Н.-Comparativestudy of various serine alkaline proteinases frommicroorganisms. Specificity with oligopeptides. Arch. Biochem. Biophys., 1971, v. 14−6, p. 297−305.
44. Xochimura S.-Proteinase from Penicillium chryzogenitna. Mem. Ну o-gо Univ. Agr-., 1962, N13, p. 42/Chem'. abstr., 1963: v. 59, ref.42ll g/.
45. Singh K.Martin S.M.-Purification and properties of a protease from Penicilliumcyaneo-fuivum. Can. J. Biochem*, I960, v. 38yp. 969−980.
46. Martin S^M., Singh K., Ankel H., and Khan A. H. -The specificity of a protease from Penicillium cyaneo-fuivum. Can. J.3iochem. ,.I962, — v. 40, p.237−246.
47. Arai M.,-and Murao S.-Purification and some properties of two alkaline proteinases from Penicillium lilacinum N2093"Agr. Biol. Chem* «1977,p. 2293−2294.
48. Belev M*, Porath J.-Extracellular proteinase from Penicilliumnotatum. 3h Methods in Enzymology, N.X.: AcaduPress., 1970, v. 19, p. 576−581.
49. Kishida T., Yoshimura S.-Mode: of action of Aspergillus ochrace-usproteinase on oxidized insulin. J. Biochem""3964*v.55*Р"95−101.
50. Danno G. f^atake M.-Substrate specificity of alkaline proteinases from Aspergillus sydowi and Aspergillus sulphurens. Agr. Biol> Chem., Д973, v. 37, p. I493-I496.
51. Dhar S.C., Bose S.M.-Studies on the specif icity of crystaline protease of Aspergillus parasiticus on j& -chain of oxidized insu*-line? and bovine serum albumin. Enzymologia, 1964, v. 28″ rp. 89−99 .
52. Nordwig A., Jahn W.F.-A colagenol^tic enzyme from Aspergillus oryzae. Purification and properties.Eur. J.Biochem., 1968, v.3"P.519.
53. Gripon J.С., Auberger В., and Lnoir J.-Metalloproteinases from Penicillium caseicolum and Penicillium roquefortii: comparison specificity and chemical characteris ation. lot. J. Biochem", 11 980, v. 32, p.451−455.
54. Nakadai T., Fasuno S, and Ijguchi N.-Purification and properties off neutral proteinase I from Aspergillus oryzae.Agr.Biol.Chem., 1973 *v.37*p. 2695−2701.
55. Roberts F.F., and Doetsh R.N.-Purification of a highly active protease-from a Microsporum species. Antonie van beeuwenhoek. J. Microbiol.Serol., 1967, v. 33"p.145−153.
56. Kandu A.K., and Manna S.-Purification and characterization of extracellular proteinases of Aspergillus oryzae.Appl.Microbiol.3375rv.30,p.?07−5l3.: :
57. Kandu A. K., Manna S., and Pal N.-Purification and properties of a new extracellular colagenase of Aspergillus sclerotionum. Indian J.Exp.Biol., 1974, v.32,p.441−443.
58. Lenney j.f., and Dalbec j.m.-Purification and propertes of a two proteinases from Saccharomyces cerevisiae.Arch.Biochem. Biophys., I967, v. 320, p.42−48.
59. Hata Т., Hayashi R., and Doi E.-Purification of yeast proteim-ses. I. Fractionation and some properties of the. proteinases. Agr. Biol. Chem., 1967, v-31,P. 150−158.
60. Hayashi R., Aibara S., and Hata T.-A unique сarboxypeptidase activity of yeast proteinase C. Biochim. Biophys. Acta, 1970, v. 232, P.359−361. :
61. Katsumxma T., Schtt E., Elsasser S., and Holzer H.-Purification and properties of tryptophan-synthase inactivating enzymes from Xeast. Eur.J.Biochem., 3372, v.27,p.520−526.
62. Cabib E., and Ulane R.-Chitin synthetase activating factor fromXeast, A protease. Biochem. Biophys. Ress, Commun., 1973, v. 50, p. 186−391.
63. Jtisic M., Hinze H., and Holzer H.-Deactivation of Xeast enzymes by proteinases A and В and carboxypeptidase X from Xeast. Hoppe Seyler*s Z.Ehysiol.Chem., 1976, v.357,p.735−740. 3.
64. Ulane R*E., and Cabib E.-The activating system of chitin synthetase from Saccharomycfs cereyisiae. Purification and properties of the activating factor. J.Biol.Chem., 1976, v.25X, p. 33 673 374.: (:
65. Saheki T., Matsuda X., and Holzer H.-Purification and characterization of maeromolecular inhibitors of proteinase A from Xeast. Eur. J. Biochem., 3974, v. 47, p. 325—332.
66. Nunez de Castro I., and Holzer H.-Studies on the proteinase A Inhibitor 13 from Xeast. Hoppe-Seiler'sZ.Physiol.Chem., 3976,•357"p.727−734.
67. Bttnning P. .MeussdoerfferF., an& Holzeir H.-Proteinase A-Inhibitors from Yeast and their application foraffinity chromatography of proteinase A. Hoppe-Seiler rs Z.Physiol. Chem. «1977,v. 358, p. II86-II87.
68. Beta, H."Hinze H., and Holzer" H.-Isolation and properties of two inhibitors of proteinase В fromYeast. J. Biol .Chem., 3974, v. 249″ PV45I5−452I.
69. Ulane R. E*, and Cabib Ei-The activating sistem of chiton synthe>-tase from Saccharomyces cerevisiae. J.Biol.Chem., 1974;249,p. 3410−3422.
70. Bfinning P., and Hblzer H.-Naturale^ occurence aid chemical modification of proteinase В Inhibitors from Yeast. J.Biol.Chem., 1977>тг.252,р.5316−5323.
71. Kuhn R.W., Kenneth A.W., and Neurath H.-Isolation and partial characterization of an acid, сarboxypept i&ase from Yeast. Biochem, New. York"I974,v. 13, p.3871−3877.
72. TOI. Hayashi R., Moore S., and Stein W.H.-Carboxypeptidase from Yeast. large scale preparation and the application to COOH-termi-nal analysis of peptides and proteins. J. Biol .Chem., 1973 «jr. 248, p.2296−2302.
73. Hay as hi R.-Carboxypeptidase Y. Methods Enzymol., I976,45B"p. 568−587.
74. Aibara B.S., Hayashi R., and Hata Ф.-Physical and chemical properties of Yeast proteinase C. Agr. Biol.Chem., ЗЭ71, v.35"P.658−666.
75. Kuhn R.W., Kenneth A. W", and Neurath H.-Reaction of Yeast car-boxypeptidase C1 with group-specific reagents. Biochemistry, New York, I976, v. 15, p.4881−4885.
76. Hay as hi R. «Bai X., and Hata T.-Evidence for an essential his-tidine in carboxypeptidase Y. Reaction with the chloromethyl ketone derivate of benzyloxy с arbonyl-I"-phenylalariin. J. Biol .Chem., 3975"*». 250, p. 5221−5226.
77. O. VoIf D.H.-Control of metabolism in Xeast and other lower eu-karyotes through action of proteinases. Adv.Micrоb.Physiol., 1980, v.2I"p. 267−338. :¦•-:
78. UI. Masuda T., Hayashi R., and Hata T.- Aminopeptidases in the acidic fractions of the Xeast autolysate. Agr. Biol.Chem., 3975, v. 39, p.499−505. о: и.
79. Frey J., and Rohm K-H. -Subcellular localization and levels of aminopeptidas es and dipeptidase in Saccharomyces cerevisiae. Bio-c hint. Biophys. Acta, 1978, v • 527, p.31−41.
80. H3.Mairi.le Ph., Wiemken A., and Guyer W.-A lysosomal aminopeptidase isozyme in diferentiating Xeast cells and protoplasts. Planta, 3971″ v. 96 $ p •43−53• :
81. Frey J., and Rohm K.H.-Peptidase of XeastrSubcellular localization and behaviour during the growth cycle. Hoppe-Seiler's Z. PhysioI.Chem., 3977"^.358,p.3202−3203.
82. H?.benney J. F.-Three Teast proteins which inhibit three Yeast proteases. Fed. Proc., 1973″ vv32, p.?59 .
83. S. Lenney J.F., Matile Ph., Fiemifcen A., SchelIenberg M., and Meyer J.
84. Activities and cellular localization of Teast proteases and theirinhibitors. Biochem. Biophys .Hess. Commun., l974, v. 60, p. 1378−1383.n.
85. H9. Hasilik A., Muller H., and Holzer H.-Compartmentation of the tryptophan-synthaseproteolyzing system in Saccharomyces cerevi-slae. Etrr. J. Biochem., 1974, v.48,p.III-117.
86. Hainbow C.-Ih «The Yeasts» /A.H.Rose and J.S.Harrison, eds/, Ac ad. Press., London, Ifew York, 1970, v. 3p. 147−224.
87. Metz G. «and Rohm K.H.-Yeast aminopeptidase I. Chemical composition and catalytic properties. Biochim.Biophys.Acta, 1976, v.429, p.933−949.
88. Kaehn K. «and Kula M.R.-Demonstration of specific aminopeptidas e inhibitors in Neurospora crassa. PEBS Lett., 1977"v.79,p.85−90.
89. Heiniger U., and Mathile P.-Protease secretion in Neurospora crassa. Biochem. Biophys «Ress. Common., 1974,^.60,p. 1425−1432.
90. Correal J. U., Rodrigues V., and Lodi W.R.-In «Limited proteolysis in Microorganisms» /G.N.Cohen and E. holzer, eds/, 1979, P* 327.
91. U.S.Government Printing office, Washington D.C.ti.
92. Hoffman W., and Hutterman.-Aminopeptidases of Physarum. poly-cephalum. Activity, isoenzyme, pattern, and synthesis during differentiation. J. Biol.Chem., 1975, T. 250, p.7420−7427.и.
93. Levins ohn S* ,-and Ar onsen A. I.-Regulation of extracellular proteases production in Bacillus cereus. J.Васteriol., 196 793, p.1023−1030.
94. Lindherg R.A. «Rhodes W.G., Eirich L.D., and Drucker H.-Extra-cellular acid proteases from Neurospora crass a. J. Bacteriol., 1982, v. 150, p. 3ZQ3-H08.
95. Eft*.Жакоб Моно Ж: Регуляторные механизмы клетки. М.: «Мир», ДЭ64, pi 273. -.: :
96. Mandelstarn J.-In" Regulation of Nucleic Acid and Protein synthesis, 1967, Amsterdam, p. 35 J.
97. Егоров H.C.-, Лория 1.К., Брюкнер В. Б. Регуляция синтеза. внеклеточных протеолитических ферментов у микроорганизмов. Успех, микроб иол. у 1977, ъх.Щ.ог 59−79.
98. Юркевич В.В.уШурыгина Н.Н.1 Механизм влияния крахмала &bdquo-на биосинтез.^-амилазы Aspergillus oryzae. — Прикл. биохим. микробиол^- 1972, т. .8, с. 5X5. «519.
99. Емцева ТЙВ-, Коновалов С. А. * Щелочные протеазы микробиологического происхождения. Прикл* биохим-1 микробиол.^ 1978, т. 14, с. 661 — 676.. ,.. .
100. Коновалов J3. АХ-биосинтез ферментов микроорганизмами. 1973, М-: Пищевая пром-ть, е.- 191.
101. Конев Л. Д. Кооперативные переходы белков в клетке. 1970, Минску 17. .
102. Hblzer ff., and Heinrich P.C.-Control of proteolysis. Annu. Rev. Biochem., 1980, v. 49, p. 63−91.
103. Drucker H.-Regulation of exocellular proteases in Neurospo-ra crassajRole of Neurospora proteases in induction. J.Bacteriol.1973• v. 116, р. 593−599.
104. Hansen R. J., Switzer R.L., Hinze H. «and Holzer H.—Effects of glucose and nitrogen source of the levels of proteinases, peptidases, and proteinase inhibitors of Yeast. Biochim.Biophys.Acta, 1977,496, p. I03-II4.
105. Holzer H.-Catabolite inactivation in Yeast. Trends Biochem. Sci., l976"v. I, p. I78-I8I.
106. Neef J."Nagele E. «Nauhaus J. «Heer U. «and Mecke: X).-Evidence for catabolite? degradation in the glucose dependent in activation of Yeast cytoplasmic malat dehydrogenase* Eur. J.Biochem., 1978, v. 87"F* 489−495 •n.
107. Prey J. «and Rohm K.H.-The glucose-induced inactivation of aminopeptidase I in Saccharomycescerevisiae. FEBS Lett., 1979* лг. 100, p. 261−264.
108. Cohen B.L., Morris J.E., and Drucker H.-Regulation of two ex-, tracelular proteases of Neurospora crassa by induction and by carbon-nitrogen and sulfur metabolite repression. Arch.Biochem. Biophys ., 1975, v. 169, P. 324−330.
109. Wolf D.H. «Ehmann C., and Beck I.-an» Biological Function of Proteinases" /H.Holzer and H. Tschesche, eds/, 1979, P.52−72.Springer verlag, Berlin, Heidelberg and New York.
110. Lenney J.F.-Three. Yeast proteins that specifically inhibit Yeast proteases A"B and C. J.Bacteriol., I975, v. I22,p.I265-I273.
111. Holzer H.-Chemistry and biology of micromolecular inhibitors from Yeast acting on proteinases A and B, and carboxypeptidase Y.
112. Mv.Ehz.Kegul.,.1975″ v. 13 «р. 125−134.
113. Pong S.S., Nuss D.L., and Koch G. -Inhibition of initiation of protein synthesis in mammalian tissue culture cells by L-I-tosyl-amido-2-pheylethyl chloromethyl ketone. J. Biol .Chem., 1975, v. 250, p. 2 240−245.
114. Rossman T., Norris G., and Troll W.-Inhibition of macromolecu-lar synthesis in Echerichia coli by protease inhibitors. Specific reversal by glutathion of the effects of chloromethyl ketones. J. Biol .Chem., 1974, v. 249, p. 3412−3417.
115. Betz: H.-Loss of sportdation ability in a. Yeast mutant with low proteinase A levels. FEBS Lett., 1979, v. 100, p. I7X-I74.
116. Mechler B. «and Wolf D.H.-Analysis of proteinase A function in Yeast. Eur. J. Biochem., l98I, v. I2I, p. A7−52.
117. Wolf D.H., and Ehmann C.-Isolation of Yeast mutants lacking proteinase В activity. FEBS Lett., l978, v.92,p.I2I-I24.
118. Jones E.W.-Proteinase mutants of Saccharomyces cerevisiae. Genetics, 197 785, p. 23−33.154,Wolf D.H., and Ehmann C.-Carboxypeptidase S-and carboxypeptidase Y-deficient mutants of Saccharomyces cerevisiae. J.Bacterid., I981, v. I47"p.A3B-426.
119. Achstetter T., Emter 0., Ehman C., and Wolf D.H.-New proteinases: in Yeast: Studies on regulation and purification. Hoppe-Sei-ler"s Z. Physiol. Chem., 1982 Bd, v. 363, p. 976.
120. Suarez Rendueles M.P., Schzencke J., Garsia Alvarez N. «and Gascon S.-A new X-prolyl-dipeptidyl aminopeptidase from Yeast associated with a particulate fraction. FEBS Lett., I98I, v. I3I, p.296−300.
121. Beck I.Fink G.R., Wolf D.H.-The intracellular proteinases and their inhibitors in Yeast. A mutant with altered regulation of proteinase A inhibitor activity. J. Biol. Chem., 1980, v. 255 *P> 4821−4828.
122. Simms P. С, and Ogrydziak D.M.-Structural gene for the alkaline extracellular protease of Saccharomyces lipolytics. J.Bacterid., I98I, v. I45*p.404−409.
123. Stewart T.W., Sherman F., Shipman N.A., and Jackson M.-Identification and mutational relocation of the AUG Codon initiating translation of Iso-I-cytochrom С in Yeast. J.Biol.Chem., 1971″ v. 246, p.7429−7445.
124. HLobel G., and Dobberstein B.-Transfer of proteins across membranes. Presence of proteolytically processed and unprocessed nascent immunoglobin light chains on membrane-boundjribosomes of murine mieloma. J. Cell. Biol., 1975, v. 67"P • 835−851.
125. Schatz G., and Mason T.L.-The biosynthesisof mitochondrial proteins. Annu.Rev.Biochem., 1974, v.43,p.51−79- :
126. Poyton O.R., and McKemmie E.-In" Limited proteolysis in microorganisms «./G.N.Cohen and Holzer H., eds/, 1979, p. 145−149. U.S.Government Printing Off ice, Washington D.C. r.
127. Duntze W., and Manney T.R.-Tvwo mechanisms of allelic complementation among Tryptophan synthetase mutants of Saccharomyces cerevisiae. J.Bacteriol., 1968, v.96,p.2085;2093.
128. Wolf D.H., and Hoffmann M.-Tryptophan synthase from Yeast. Purification by affinity chromatography, physical properties. Eur.
129. J.Biochem., 1974, v.45,p.268−276.
130. Matchett W.H.and De Moss J. A.-The subinit structure of tryptophan synthase from Neurospora crassa. J.Biol.Chem. «1975,v.250, p*2941−2946.
131. Giles N.H., Case M.E., Partridge C.W.H., and Ahmed S.I.-A gene cluster in Neurospora crassa coding for an aggregate of five aromatic synthetic enzymes. Proc.Natl. AcacUSci.XT.S.A., 1967, v.58,p. 1455−1460.
132. Gaertner F.H.-Purification of two multienzyme complexesin t~ he aromatic/Erypthophan pathway of Neurospora crassa. Arch. Biochem. Biophys. «1972,v. 151, p. 277−284.
133. I. Gaertner F.H., and Cole K.W.-The protease problem in Neurospora, Structur al modification of the arom multienzyme system during Its extraction and isolation. Arch.Biochem.Biophys."3976"v. 177"P. 566−573.
134. Duran A* «Bowres B. «and Cabib E.-Chitin synthetase zymogen is attached to the Yeast plasma membraneProc.Natl.Acad.Sci.U.S.A., 1975, v.72,p.3952−3955.
135. RuiZf-herrera J., Romero E.L. «and Bartnicki-Garcia S.-Properties of chitin synthetase in isolated chitosomes from Yeast cells of Mucor rouxii. J.Biol.Chem., 1977, v.252,p.3338−3343.
136. Cellini-Вгагт P. «and Calderon R.A.-Chitin synthetase in Candida albicans: comparison of Yeast and Hyphal forms. J.Bacteriol., 1978,^r. 133, P. 1472−1477.
137. Zubenko G. S"Mitchell A. P", and Jones E.W.-In «limited proteolysis in Microorganisms» /G.H.Cohen and H. Holzer, eds/, 1979, p.49−53. U.S.Government Printing Office, Washington, D.C.
138. Matern H., and Holzer H.-Catabolite inactivation of the Galactose uptakesystem in Yeast. J.Biol. Chem1977, v.252,p.6399−6402.
139. Witt I., Kronau R. ,-and Holzer H.-Repression von alkobole-dehi-drogenas e, mal atdehydrogenase, isocitr at lyaseund malat synthase in hefe durch glycose. Biochim. Biophys. Acta, 1965, v. 118, p. 552−537.
140. Gancedo C.-Inactivation of fructose-I, 6-diphosphatase by glucose in Yeast. J.Bacteriol., 3371"V.I07,p.401−405. '.
141. Haarasilta S., and Oura E.-Qn the activity and regulation of anaplerotic and glucmeogenetic enzymes during the growth process of Baker’s Yeast. The biphasic growth. Eur.J.Biochem., 197 552"p. 1−7.
142. Gancedo C., and Schwerzmann N. In activation by glucose of phosphoenolpiruvate с arboxy kinase from Saccharomyces cerevisiae. Arch. Microbiol., 1976, v. 109 &bdquo-Р* 221−225.
143. Molano) J., and: Gancedo C.-Specific deactivation of fructoso-1,6-biphosphatase from Saccharomyces cerevisiae by a Yeast protease. Ешг. J, Biochem*, ЗЭ74, v. 44, p* 233−217.
144. Waif D.H. «and Ehman C.E.-Studies on a proteinase В mutant of Yeast. Eur.J.Biochem., ЗЭ79"v.98,p"375−384.l93.Sussman A.J."and Gilvarg G.-Peptide transport and metabolism in bacteria. Annu.Rev. Biochem. «1971, v. 40, p. 397−408'.
145. Goldberg A.L., and St. John A.C.-IntraceIluiILar protein degradation in mammalian and bacterial cells. Part II. Annu. Re v. Biochem., ЗЭ76, v. 45, p •747−803•.
146. Hopper A. K", Magee P.T., Welch S.K., Friedman M. «and Hall B.D.-Macromolecule synthesis and breakdown in relation to sporulation and meiosis in Yeast. J, Bacterial., 1974*v. H9, p.619−628.
147. Wolf D.H., and Ehmann G.-Carboxypeptidase S from Yeast: regula-tion of its activity during vegetative growth and differentiation. FEBS Lett., 3978, v. 91, P. 59−62.
148. Correa J.U., Iiemos E.M., and Lodi W.R.-Inhibition of sporulation in the water mold Blastocladiella emersonii by antipain. Dev.Biol. 1978"v.66,p.470−479.
149. ОЗ. Билай В. И. -Основы общей микологии: Учеб. пособие для вузов. Киев: Вшца. школа,. 1980.' — .
150. Лобарева Л. С., .Степанов В.-М., Карбоксильные протеиназы. плесневых, грибов. В кн.: Успехи биол. химии, М.: Наука, 1978, т. 39, с. 83−105.: :
151. Data for biochemical research.Oxford.At the clarendon press. Ed. by Dawson R.M.C., Elliott D.C., Elliott W.H., and Jones K.M.I969.
152. Lowry 0. H., Rosebrough H.J., Farr A. L., and Randall R.J.-Protein measurement with the folin phenol reagent. J, Biol. Chem,, 1951"v. 393, p. 265−275.: ;
153. Laemmli U.K.-Cleavage of structure proteins during assembly of the head of bacteriophage T4. Nature «London, I970"v. 69"p.646−651.
154. Besses O.A., Lowry O.H., Love R.G.H.-The fluorometric measurement of the nucleotides of. riboflavin and their concentration in tissues. J. Biol .Chem. «1949 «v. I80"p. 755.
155. Whitaker J.R. -Determination of molecular weights of proteins by gel filttration on Sephadex.-Anal.Chem* «1963 «v. 35, p. 1950;1953•.
156. Coben В.Ь.-The proteases of Aspergilli, 1977"p. 281−293. 3n J. eI^ i.
157. Smith, and J.A.Pateman /eds/, Genetics and physiology of Aspergilli.us. Academic. press, Iiic., New York.,. ,.
158. Колтун Л^ВЦШавловокий Кащенко В*-Е-у. Трач В. М* Изменение активнооти некоторых ферментов флавиногенеза в процессе культивирования гриба Eremothecium ashbyii. Микробиология^ 1984, т. 53, о. 43 ~ 46.
159. Burgum A. A. «and Prescot J.М.-Isolation and characterization of fungal endopeptidase. Arch.Biochem. Biophys•, 1965 «v. Ill, p. 39 139®.
160. Danno G., and Yoshimura S.-Studies on an alkaline proteinases of Aspergillus sydowi. Part I. Purif ication and. some properties of proteinase. Agr.Biol.Chem., vl967″, v.3I*P.H5l-H5S.
161. Gaucher G.M., and Stevenson K. J.-Thermomycolin. In methods in enzymology, N. Y.: Acad. Press, 1979"T. 45 «P • 415−433.
162. Viccardo J. R. -Pur if ic at ion * cry s t al lyz ation and composition of an alkaline proteinase from Cephalosparium sp. 30. Diss.Abstr. Int. «ser. BfJI969 «v. 29, p. 3420.
163. Morihara K., and Tsuzuki H—Specificity of proteinase К from Tritirachium album Limber for synthetic peptides. Agr.Biol.Chem. 3975,>v.39,p.IW-I492.
164. Hay as hi K., Fukushima D., and Modi K.-Alkaline proteinase of Aspergillus sо3ae. Phys icochemical properties «amino acid composition andmolecular conformation. Agr. Biol.Chem., I967"v.3I"p.642−643.
165. Докл.- АН. СССР, 1976, — т. 230, с.1485 1487.
166. Караваева Н.Н.^,. Закиров М. З., Мухиддинова Н. Г. Частичная очистка и некоторые свойства протеазы гриба Torula thermophila Биохимия, — 1975, т. .40, с. .909 — .914.
167. Тривен. M. iИммобилизованные ферменты. Вводный курс и применение в биотехнологии. М.: «Мир», 1983. .