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1.
Mikrobiologiia ; 85(2): 171-6, 2016.
Artigo em Russo | MEDLINE | ID: mdl-27476205

RESUMO

Production of proteinases with plasmin-like and plasminogen-activating activities by a micromycete Arthrobotrys longa 1 was studied. Polycyclic growth of the producer in submerged cultures was observed, with an endogenous rhythm of the periods of intense microconidia formation alternating with the phases of drastic increase in the content of producing mycelium. The highest plasminogen-like and plasminogen-activating activities (up to 1000 and 500 cond. U/mL, respectively) were found to correlate with the polycyclic growth of the producer, coinciding with the stage of microconidia germination. Enhanced secretion of proteinases with plasminogen-like and plasminogen-activating activity was found to be associated with increased specific growth rate of A. longa l.


Assuntos
Ascomicetos/enzimologia , Proteínas Fúngicas/biossíntese , Micélio/enzimologia , Peptídeo Hidrolases/biossíntese , Humanos , Terapia Trombolítica
2.
Mikrobiologiia ; 84(3): 316-22, 2015.
Artigo em Russo | MEDLINE | ID: mdl-26263691

RESUMO

Screening for producers of proteinases with fibrinolytic (plasmin-like and plasminogen-activating) and collagenolytic activities-was carried out among 83 strains of microscopic fungi belonging to various ecological groups. Entomopathogenic micromycetes secreted proteinases with higher fibrinolytic and collagenolytic activity than saprotrophic, potentially phytopathogenic, and epiphytic strains. Micromycete strains possessing proteolytic enzymes with collagenase activity were revealed, as well as the strains producing proteinases with plasmin-like activity. None of the strains studied secreted proteinases possessing only plasminogen-activating activity. Tolypocladium inflatum k1 was found to be a producer of extracellular proteinases with high plasminogen-activating, plasmin-like, and collagenolytic activities. The specific plasminogen-activating activity of T. inflatum k1 was shown to be 20% higher than its plasmin-like activity.


Assuntos
Ascomicetos/enzimologia , Colagenases/química , Fibrinolíticos/química , Proteínas Fúngicas/química , Colagenases/metabolismo , Fibrina/química , Fibrinolisina/química , Proteínas Fúngicas/metabolismo , Gelatina/química , Ensaios de Triagem em Larga Escala , Hidrólise , Ativadores de Plasminogênio/química
3.
Prikl Biokhim Mikrobiol ; 51(1): 86-92, 2015.
Artigo em Russo | MEDLINE | ID: mdl-25842908

RESUMO

The properties of an extracellular proteinase activating plasma protein C isolated from the culture supernatant of A. ochraceus VKM F-4104D have been studied. This enzyme demonstrated a substrate specificity absent of hydrolyzing activity toward chromogenic proteinase substrates. On the basis of inhibitory analysis, the protein C-activating proteinase from A. ochraceus VKM F-4104D appeared to be a serine proteinase, together with that isolated from the venom of Agkistrodon contortrix contortrix. The isolated enzyme was a nonglycosylated protein with a molecular weight of about 33 kDa, pI 6.0 with an observed optimal activity under a pH of 8.0-9.0 and 37°C. A comparison of the properties of the protein C-activating proteinase formed by A. ochraceus and the enzyme derived from the venom of Agkistrodon contortrix contortrix demonstrated a similarity in their properties; however, proteinase from the micromycete appeared to be in the nonglycosylated state and possessed the ability to hydrolyze the chromogenic plasmin substrate H-D-Val-Leu-Lys-pNA.


Assuntos
Aspergillus ochraceus/enzimologia , Serina Proteases/química , Serina Proteases/isolamento & purificação , Humanos , Peso Molecular , Plasma/química , Proteína C/química , Proteína C/metabolismo , Serina Proteases/genética , Inibidores de Serina Proteinase/farmacologia , Venenos de Serpentes/enzimologia , Especificidade por Substrato
4.
Prikl Biokhim Mikrobiol ; 50(3): 245-55, 2014.
Artigo em Russo | MEDLINE | ID: mdl-25757332

RESUMO

Specific features in the development of micromycetes, typical mechanisms of their enzyme production, and conditions providing for an increase in enzyme secretion by the microscopic fungi in solid-state (on natural substrates and inert carriers) and membrane-surface liquid cultures are considered. The prospects and advantages of these fermentation methods for the production of extracellular enzymes are discussed and compared with submerged cultures.


Assuntos
Proteínas Fúngicas/isolamento & purificação , Hifas/enzimologia , Fungos Mitospóricos/enzimologia , Técnicas de Cultura de Células , Meios de Cultura/química , Fermentação , Proteínas Fúngicas/biossíntese , Hifas/crescimento & desenvolvimento , Fungos Mitospóricos/crescimento & desenvolvimento
5.
Bioorg Khim ; 40(6): 688-94, 2014.
Artigo em Russo | MEDLINE | ID: mdl-25895365

RESUMO

Screening of the genus Aspergillus micromycetes for secretion of extracellular proteolytic enzymes, capable of acting on human proteins of the hemostatic system, has been conducted. The ability of extracellular proteases of Aspergillus to cleave specific proteins of the hemostatic system chromogenic peptide substrates, as well as activate a series of proenzymes (protein C, factor X and prothrombin) has been found. The ability of extracellular proteases of micromycetes activate X factor of human blood plasma was first shown at the first time.


Assuntos
Aspergillus/enzimologia , Fator X/metabolismo , Hemostasia , Peptídeo Hidrolases/química , Fator X/química , Humanos , Peptídeo Hidrolases/metabolismo , Peptídeos/química , Proteína C/química , Proteína C/metabolismo , Protrombina/química , Protrombina/metabolismo
6.
Prikl Biokhim Mikrobiol ; 49(6): 580-6, 2013.
Artigo em Russo | MEDLINE | ID: mdl-25434181

RESUMO

The conditions for the submerged and solid-state cultivation of the micromycete Aspergillus ochraceus VKM F-4104D, producing extracellular proteinases that activate protein C in human blood plasma, were optimized. It is shown that the protein C-activating activity of the micromycete in a solid-state culture was 1.5-3.5 times higher than in a submerged culture (as calculated per milliliter of culture medium). Among the extracellular proteins secreted by A. ochraceus VKM F-4104D during submerged and solid-state cultivation, a protein C-activating proteinase with a pI of 6.0-6.3 was identified.


Assuntos
Aspergillus/enzimologia , Proteínas Fúngicas/metabolismo , Peptídeo Hidrolases/metabolismo , Plasma/química , Proteína C/química , Proteínas Fúngicas/química , Humanos , Peptídeo Hidrolases/química
7.
Prikl Biokhim Mikrobiol ; 48(5): 537-42, 2012.
Artigo em Russo | MEDLINE | ID: mdl-23101392

RESUMO

Natural isolates of Aspergillus ochraceus myxomycetes from soil and plant remains from various regions have been screened. The isolated strains were characterized by similar cultural and morphological features and an identical nucleotide sequence in the ITS1-5,8S-ITS2 region of rDNA. The ability of the extracellular proteinases of A. ochraceus myxomycetes to activate protein C of blood plasma has been established. Differences are revealed in the accumulation of proteinases activating protein C and proteinases with thrombin- and plasmin-like activities in the growth dynamics of producers.


Assuntos
Aspergillus ochraceus/metabolismo , Peptídeo Hidrolases/metabolismo , Proteína C/metabolismo , Aspergillus ochraceus/genética , DNA Ribossômico , Espaço Extracelular/química , Espaço Extracelular/metabolismo , Fibrinolisina/metabolismo , Humanos , Plasma , Homologia de Sequência do Ácido Nucleico , Trombina/metabolismo
8.
Mikrobiologiia ; 77(3): 318-23, 2008.
Artigo em Russo | MEDLINE | ID: mdl-18683647

RESUMO

Population growth, the ratio between dissociants, pH, and levels of reducing sugars in the medium were monitored during prolonged (375 h) batch cultivation of Pseudomonas aeruginosa S and M dissociants on mineral medium with glucose. During the stationary growth phase (100-375 h), two scenarios were possible. The first one included extensive cell autolysis coupled to alkalinization of the medium and an increased ratio of the M dissociant. In the second case, acidification of the medium was coupled to the oscillating secondary growth, mostly of the M dissociant; the dynamics of cell numbers of this dissociant correlated with the dynamics of the culture optical density. In this scenario, periodical appearance of reducing sugars in the medium was detected; it was in the opposite phase with the changes of the M dissociant cell numbers. The differences between scenarios of P. aeruginosa growth in the late stationary phase were probably due to the physiological and biochemical characteristics of the S and M dissociants, including different pathways of glucose utilization (respiration or fermentation), resistance to acidification, synthetic (proteolytic) activity, and productivity of autoinducers.


Assuntos
Pseudomonas aeruginosa/crescimento & desenvolvimento , Bacteriólise , Técnicas de Cultura de Células , Meios de Cultura , Fermentação , Glucose , Concentração de Íons de Hidrogênio , Oxirredução , Pseudomonas aeruginosa/citologia , Pseudomonas aeruginosa/metabolismo , Fatores de Tempo
9.
Antibiot Khimioter ; 47(4): 3-6, 2002.
Artigo em Russo | MEDLINE | ID: mdl-12369143

RESUMO

The method of lovastatine and mevinolinic acid known as competitive inhibitors of HMG-CoA-reductase and produced by micromycetes was elaborated. The inhibitors from diluted water solutions were fully absorbed on Diapak C16 patrons. The rate of inhibitors elution from the patrones was more than 95 per cent. Patrons may be used for concentration of lovastatine group inhibitors from the culture media. Inhibitors synthesis by the Penicillium citrinum 89 was investigated in dynamics with the use of Diapak C16 patrones. It was shown that UV-spectrum of inhibitor produced by P. citrinum 89 was identical with compactin spectrum and had absorbance maximum at 230, 237 and 247 nm.


Assuntos
Inibidores de Hidroximetilglutaril-CoA Redutases/isolamento & purificação , Lovastatina/análogos & derivados , Lovastatina/isolamento & purificação , Penicillium/metabolismo , Esteróis/antagonistas & inibidores , Cromatografia/métodos , Soluções
10.
Antibiot Khimioter ; 47(1): 3-6, 2002.
Artigo em Russo | MEDLINE | ID: mdl-12077938

RESUMO

Antifungal activity of micelial fungus metabolites (of genera Aspergillus, Penicillium, Fusarium, Stachybotris, Cladosporium, Alternaria, Gliocladium, Paecilomyces, Trichoderma etc.) was determined. It was shown that antifungal activity of some micromycetes is due to the formation of substances inhibiting sterols biosynthesis in eucaryote cells. Inhibitors of enzymes of sterols biosynthesis were isolated and their activity was investigated. It was shown, that isolated fungus inhibitors of sterols biosynthesis inhibited the growth of test-organism Rhodotorula rubra and decreased ergosterin level in yeast cells. The qualitative content of yeast cell sterols was not changed in the presence of fungus inhibitors.


Assuntos
Ergosterol/biossíntese , Inibidores do Crescimento/isolamento & purificação , Fungos Mitospóricos/metabolismo , Rhodotorula/efeitos dos fármacos , Inibidores do Crescimento/metabolismo , Fungos Mitospóricos/química , Rhodotorula/crescimento & desenvolvimento , Rhodotorula/metabolismo
12.
Antibiot Khimioter ; 40(8): 12-6, 1995 Aug.
Artigo em Russo | MEDLINE | ID: mdl-8713431

RESUMO

The action of lovastatin, a competing inhibitor of 3-hydroxy-3-methylglutaryl CoA reductase, on bacterial bioluminescence was studied. The lovastatin lactone form and sodium salt of mevinolinic acid inhibited bacterial luciferase in vitro but did not affect bioluminescence of the intact cells of the luminous bacteria. The inhibition was found to be of a competing character in regard to aliphatic aldehyde, the bacterial luciferase substrate. Conditions under which the bioluminescence inhibition was proportional to the lovastatin concentration in the incubation mixture and a bioluminescence method for quantitative determination of the inhibitor were developed.


Assuntos
Anticolesterolemiantes/farmacologia , Colesterol/biossíntese , Inibidores Enzimáticos/farmacologia , Lovastatina/farmacologia , Medições Luminescentes , Vibrio/efeitos dos fármacos , Inibidores de Hidroximetilglutaril-CoA Redutases , Luciferases/antagonistas & inibidores , Luciferases/isolamento & purificação , Estrutura Molecular
13.
Biokhimiia ; 52(12): 2002-8, 1987 Dec.
Artigo em Russo | MEDLINE | ID: mdl-3447630

RESUMO

Extracellular carboxypeptidase was isolated from culture filtrates of Str. spheroides strain 35, using affinity chromatography on bacitracin-silochrome, bacitracin-Sepharose and CABS-Sepharose. The electrophoretically homogenous enzyme was obtained with a 44% yield and 4160-fold purification. The enzyme-molecular weight is 33,000 Da; pI is 4.7. The amino acid composition of carboxypeptidase is as follows: Asp43, Thr30, Ser35, Glu33, Pro30, Gly47-50, Ala38, 1/2 Cys5-6, Val16, Met2, Ile11, Leu15, Tyr8, Phe10, Lys10, His6, Arg9. The enzyme shows an activity optimum at pH 7.5 is stable at pH 6-8, is completely inhibited with EDTA and can be reactivated by Ca2+. The carboxypeptidase from Str. spheroides strain 35 has a dual substrate specificity, i. e., it splits N-substituted di-, three- and tetrapeptides having both neutral and basic amino acids at the C-ends similar to mammalian carboxypeptidases A and B. The enzyme belongs to the family of metallocarboxypeptidases; its properties are very similar to those of carboxypeptidase S from Str. griseus K-1 and of carboxypeptidase T from Thermoactinomyces sp.


Assuntos
Carboxipeptidases/isolamento & purificação , Streptomyces/enzimologia , Aminoácidos/análise , Carboxipeptidases/metabolismo , Cromatografia de Afinidade , Eletroforese em Gel de Poliacrilamida , Concentração de Íons de Hidrogênio , Focalização Isoelétrica , Cinética , Peso Molecular , Especificidade por Substrato
14.
Biokhimiia ; 48(8): 1365-73, 1983 Aug.
Artigo em Russo | MEDLINE | ID: mdl-6354275

RESUMO

A serine proteinase possessing a fibrinolytic activity was isolated from a culture filtrate of Streptomyces spheroides, strain 35. A consecutive use of affinity chromatography on bacillichin-silochrome and bacitracin-sepharose and ion-exchange chromatography on anionie PAP and cationic KMT resulted in a homogeneous proteinase with 1060-fold purification and 19% yield. The enzyme has a molecular weight of 28000; its amino acid composition is Asp31, Ser28, Thr29, Glu9, Pro14, Gly35, Ala42, Val26, Ile14, Leu13, Met2, Tyr9, Phe4, Trp3, His6, Lys4, Arg10. The enzyme has a pI at pH greater than 10 and the activity optimum against Z-L-Ala-L-Ala-L-Leu-pNA at pH 10-11. The enzyme is stable within the pH range of 4-11 and in 6 M guanidinium chloride pH 8.0 in the presence of Ca2+. The enzyme is inhibited by diisopropylfluorophosphate and benzylsulfofluoride, specific inhibitors of serine proteinases as well as by potato proteinase inhibitor. The serine proteinase SSPB isolated from Str. spheroides, strain 35 can be related to subtilisin-like serine proteinase, especially to those of SGPD and SGPE of Str. griseus.


Assuntos
Endopeptidases/isolamento & purificação , Streptomyces/enzimologia , Aminoácidos/análise , Concentração de Íons de Hidrogênio , Cinética , Peso Molecular , Serina Endopeptidases , Especificidade por Substrato
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