[Specific control over the synthesis of plasmin-like and plasminogen-activating proteinases in marine bacteria]. / Osobennosti kontrolia sinteza proteinaz s plazminopodobnoi i aktivatornoi aktivnostiami u morskikx bakterii.

The biosynthesis of proteinases with various substrate specificities was studied in Bacillus firmus 44b and Bacillus oligonitrophilus 21p as influenced by the growth conditions and growth phases of the bacteria. The period of the maximum synthesis of plasmin-like enzymes was observed 6 h later than the period of the maximum growth rate period of B. firmus 44b, and 3 h as compared to the growth rate of B. oligonitrophilus 21p. The periods of the maximum accumulation of activating enzymes were delayed 9 and 12 h, respectively, as compared to the rapid growth periods of these two bacteria. Catabolite repression of proteinase synthesis and stimulation of the latter with substrate proteins were insignificant. The production of both plasmin-like and plasminogen-activating enzymes was most sensitive to repression by nitrogen deficiency. The production of plasminogen-activating proteinases was less dependent on the carbon source than the production of plasmin-like enzymes.

[Micromycetes extracellular proteinases with fibrinolytic and anticoagulant properties]. / Ekstratselliularnye proteinazy mikromitsetov s fibrinoliticheskimi i antikoaguliantnymi svoistvami.

One hundred and sixteen strains of microscopic fungal belonging to different taxonomic groups were tested for their ability ti synthesize extracellular proteinases with caseinolytic, fibrinolytic, plasminogen activator-like, and anticoagulant (prolonging the partial thromboplastin time) activities. Several producers of anticoagulants prolonging the partial thromboplastin time, probably via the activation of the protein C system, were revealed. The effectiveness of the fungal anticoagulants was close to that of the protein C activators from Agkistrodon snake venom.

[Mitochondrial ribosomes of the phytoflagellata Astasia longa]. / Ribosomy mitokhondrii fitoflagelliata Astasia longa.

The physico-chemical properties of ribosomes and rRNA isolated from the mitochondria of the phytoflagellata Astasia longa were studied. It was shown that the mitochondrial ribosomes of A. longa have the sedimentation coefficient of 81S (those of the cytoplasm-82S); upon a decrease of Mg2+ concentration in the medium they dissociate into subparticles with sedimentation coefficients of 60 and 45S. The relative protein content in the mitochondrial ribosomes of A. longa is equal to 42% (rho = 1,60 g/cm3), that of cytoplasmic ribosomes-49%. The molecular weights of mitochondrial rRNA are equal to 1,05 . 10(6) and 0,71 . 10(6) and differ from those for cytoplasmic rRNA (1,32 . 10(6) and 0,94 . 10(6)). It was shown that the GC-content in mitochondrial rRNA is equal to 32,0 mol. %, that in cytoplasmic rRNA-55,9 mol. %. Thus, the mitochondrial ribosomes of A. longa differ in some of their properties from both procaryotic and eucaryotic ribosomes and are probably related to a special type of mitochondrial ribosomes.

[Ribosomes of the blue-green alga Anabaena variabilis. Sedimentation, density characteristics and analysis of ribosomal RNA]. / Ribosomy iz sine-zelenoi vodorosli Anabaena variabilis. Sedimentatsionnaia, plotnostnaia kharakteristika i analiz ribosomal'nykh RNK

Ribosomes and rRNAs were isolated from cells of green-blue alga Anabaena variabilis. The sedimentation properties of the ribosomes as well as density, molecular weights and nucleotide composition of rRNAs were determined. The ribosomes were found to have the S20,w value equal to 67.2+/-0.4S, whereas those of the ribosome subunits were 48.6+/-0.8 and 29.5+/-1.1S. The buoyant density of the ribosomes in CsCl was 1.641+/-+/-0.002 g/cm3; a calculated relative protein content was 35%. The molecular weights of rRNAs estimated by electrophoresis in PAAG containing 0.5% agarose, are 1.1-10(-6) and 0.56-10(6) daltons. The nucleotide composition of rRNA was determined and rRNA was shown to belong to the GC type. Consequently, the blue-green alga ribosomes do not differ in the parameters studied from bacterial ribosomes.