[Morphological and Physiological Properties of the Micromycete Arthrobotrys longa, a Producer of Longolytin, a Proteolytic Complex with a Thrombolytic Effect].

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.

[Screening of Producers of Proteinases with Fibrinolytic and Collagenolytic Activities among Micromycetes].

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.

[Effect of extracellular proteases of micromycetes of the genus Aspergillus on proteins of haemostasis system].

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.

[Properties of extracellular proteinase--an activator of protein C in blood plasma formed by Aspergillus ochraceus].

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.

[Solid-State and membrane-surface liquid cultures of micromycetes: specific features of their development and enzyme production (a review)].

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.

[Production of extracellular proteinases (protein C activators in blood plasma) by the micromycete Aspergillus ochraceus during submerged and solid-state cultivation].

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.

[Aspergillus ochraceus myxomycetes produce extracellular proteinases--protein C activators of blood plasma].

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.

[Development and population structure of mixed (S + M) Pseudomonas aeruginosa cultures in the late stationary growth phase].

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.

[Concentration on Diapak C 16 capsules of lovastatin, mevinolinic acid and other inhibitors of biosynthesis of sterins produced by Penicillium citrinum 89].

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.

[Micromycetes metabolites--inhibitors of growth and sterol biosynthesis in yeasts].

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.

[Action of lovastatin--an inhibitor of cholesterol biosynthesis on bacterial bioluminescence].

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.

[Isolation and properties of carboxypeptidase from Streptomyces spheroides, strain 35].

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.

[Subtilisin-like proteinase SSPB from Streptomyces spheroides, strain 35].

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.