PubMed Health⌕ Search

Biomedical subjects

O S Tsiperovich

Publications and source records attributed to O S Tsiperovich.

7 recordsLinked to original sources
PubMedDate not supplied

[Chymotrypsin-like proteinases in microbial proteolytic complexes].

A considerable amount of proteinase of chemotrypsin type (AO-ct) was found in the proteolytic system of Asp. oryzae, strain "h"-476. The proteinase produces an intensive effect when hydrolyzing p-nitrophenyl acetate (p-NPA) -- 18-20 times as strong as that of crystalline chemotrypsin. Comparison of the AO-ct and chemotrypsin properties resulted in proving the enzyme nature of the p-NPA hydrolysis reaction. A study of AO-ct specificity with the presence of such substrates as p-NPA, o-nitro-phenyl acetate, 2,4,dinitrophenyl acetate (2,4-DNP) showed that displacement of the nitrogroup into the ortho-position produces a 4-fold inhibition in the hydrolysis, introduction into the molecule of other nitrogroup (2,4-DNP) -- a 9-10 fold inhibition, the effect of chemotrypsin on them is considerably weaker, but 2.4-DNP hydrolyses more intensively. Definite differences are found in the effect of AO-ct and chemotrypsin in hydrolysis of phenyl acetate, N-benzoyl-tyrosine-methyl ester and casein. All the reactions are completely inhibited with DFP. The esterolytic activity (substrate p-NPA) is detected in a series of the exocellular proteolytic complexes, their effect being rather intensive but diverse.

Aspergillus↗
PubMedDate not supplied

[Gelatin from bone collagen hydrolyzed with Streptomyces griseus protease and its properties].

Gelatin melting from bone collagen previously hydrolyzed with the Str. griseus protease was studied as dependent on the medium temperature. The properties of this gelatin were compared with those of others melted from collagen previously extracted with alkali. Gelatin obtained by using the Str. griseus protease has the average molecular weight of 63 400 characteristic viscosity of 0.22, it contains 10.6% of oxyproline and 0.06% of free carbohydrates. By a degree of heterogeneity the preparation obtained does not differ from those used for the comparison.

Bone and Bones↗
PubMedDate not supplied

[Effect of deuteration on some IR-spectral characteristics of gelatin].

The IR-spectra of normal and deuterated gelatin samples were studied. The 3300 cm-1 band is determined by the valence vibrations of the peptid bond NH-groups, OH-groups of oxyproline and structural water. The 1280-1220 cm-1 bands cannot be intepreted for gelatin as amide III; their appearance is caused by the skeleton vibrations. The 1460 cm-1 band is not Amide II in gelatin, it is associated with the deformation vibrations in free methyl groups of the amino acid residues. The effect of OH-groups of hydration water forming the intramolecular hydrogen bond is displayed by 1670 cm-1 band. Disappearance of the 1560 and 1530 cm-1 bands with deuterating and appearance of the 1580 cm-1 band may evidence for a structural transition of the gelatin molecule from one conformation to another, is more ordered, conformation.

Amino Acids↗
PubMedDate not supplied

[Carboxypeptidases from different microbiolorganisms].

Experiments were performed to detect "alkali" and "acid" carboxypeptidases in 39 enzymic preparations from fungi, yeast, actinomyces, bacteria and algae. Distribution of both types of carboxypeptidases is different: they are absent in the six of the studied sources, there are no "acid" carboxypeptidases in 11 sources and no "alkali" in nine ones. The largest amount of carboxypeptidases is in the objects from fungi and actinomycetes, the least, in those from bacteria and algae. There is no correlation between synthesis of these enzymes by one microorganism. Thus, fungi produce mainly "acid" enzymes, and actinomycetes only "alkali" ones. Asp. oryzae and Asp. flavus are powerful producers of the former, Streptomyces griseus of the latter. Specific activities 15-20 times as high as all the already studied ones are obtained for the preparations isolated from Str. griseus (protezym, proteinase-1, proteinase-3, crystal line complex of proteases). Carboxypeptidase of Str. griseus is relatively stable in comparison with "acid" ones in purification and concentration.

Actinomyces↗