[Soluble caruncle proteins in pregnancy]. / Rastvorimye belki karunkulov pri stel'nosti.

Solvable proteins of caruncles have been studied at pregnancy. A group of solvable proteins absent in the blood serum, amniotic fluid, fetal placenta and uterus mucosa independent of the phase of ovary development is revealed. Molecular weight of most of them is 40 kDa. It is supposed that the found proteins take part in embryogenesis.

[Characteristics of the protein spectrum of bovine amniotic fluid]. / Osobennosti belkovogo spektra amnioticheskoi zhidkosti korov.

When studying peculiarities of the protein composition of amniotic fluid in cows a group of proteins with molecular mass below 60 kDa was found. There are no such proteins in blood of those animals. It is supposed that these proteins can take active part in embryogenesis processes.

[Effect of proteolytic inhibitors from human plasma on the activity of native and immobilized terrilytin]. / Vliianie proteoliticheskikh ingibitorov plazmy krovi cheloveka na aktivnost' nativnogo i immobilizirovannogo terrilitina.

Human blood plasma inhibitors are studied for their effect on the activity of terrilytin, a proteolytic enzyme of microbial origin, and terridecase, its immobilized form. The main plasma inhibitor of terrilytin is alpha 2-macroglobulin (alpha 2 MG). The pattern of terrilytin and terridecase interaction with alpha 2 MG preparation isolated from human blood plasma has also been studied. The inhibitor is found to exert a slight retarding effect on the terridecase activity. Significant differences in alpha 2 MG inactivation of terrilytin and trypsin are observed.

[Effect of levamisole on alpha 2-macroglobulin and lysozyme levels in the trachea, peritoneal exudate and serum of mice]. / Vliianie levamizola na uroven' alpha2-makroglobulina i lizotsima v trakhee, peritoneal'nom ékssudatei syvorotke krovi myshei.

Levamisole was studied for its effect on alpha 2-macroglobulin and lysozyme content in the blood serum, peritoneal exudate, tracheal extracts of mice. Dynamics of changes in the content of these proteins was studied with its significant increase depending on the methods of the preparation administration (inhalation; intraperitoneal and per os).

[Prospects of applying immobilized enzymes in medicine]. / Perspektivy primeneniia immobilizovannykh fermentov v meditsine.

The paper deals with evidence on main trends for using immobilized enzymes in medicine. The lyposomes are shown to be means for delivering enzymes to a cell under certain hereditary diseases. The prospects are considered for using the bound enzymes for treating some pathologic processes (py0-inflammatory, thrombosis, malignant tumors, etc.). The data are presented on possibilities of applying the immobilized enzymes as specific reagents for determining substrates and metabolites in the disease diagnostics.

[Study of bone tissue insoluble collagen hydrolysis by Streptomyces griseus protease using the method of N-terminal analysis]. / Doslidzhennia metodom N-kintsevogo analizu gidrolizu nerozchinnogo kolagenu tkanini kistok proteazoiu Streptomyces griseus.

Str. griseus protease hydrolyzes essentially insoluble collagen of bone tissue, with 34.5% of protein solubilized and 6.0% of peptide bonds splitted. 60.0 M of N-terminal amino acids is formed per 10(5) g of protein, out of them 16.8 in the fraction of free amino acids, 32.3 M in the fraction of soluble DNP-peptides and 10.9 M in that of insoluble DNP-peptides. Under the effect of trypsin the amount of collagen changing to the soluble form is thrice as low and the splitted peptide bonds are ten times as low as in case of the Str. griseus protease action. The peptide bonds incorporating the N-end of serine, threonine, glycine are more available for protease. It is supposed that under used conditions Str. griseus protease hydrolyzes not only telepeptides but also the main molecule of collagen.

[Hydrolysis of insoluble bone collagen by crystalline alpha-amylase from Aspergillus oryzae]. / Hidroliz nerozchynnoho kolahenu kistok krystalichnoiu al'fa-amilazoiu z Aspergillus oryzae

The paper deals with hydrolysis of bone collagen thrice recrystallized alpha-amylase. The enzyme action was estimated by the amount of released glycopeptides, free carbohydrates, alpha-amine groups and total nitrogen in the soluble part of the hydrolyzate. The protease admixture in the alpha-amylase preparation was found by means of the Aspergillus oryzae protease. The data obtained testify to the fact that hydrolysis of collagen under the effect of crystalline alpha-amylase occurs only due to the protease admixture in the amylolitic preparation. When an attempt was made to obtain acid-soluble collagen from bone insoluble collagen previously treated with the alpha-amylase preparation, it was found that under these conditions bone collagen, as distinct from skin collagen, is not solubilized in diluted acetic acid.

[Study of gelatin hydrolysis by Streptomyces griseus protease using the method of N-terminal analysis]. / Dsolidzhennia metodom N-kinstevoho analizu hidrolizu zhelatynu proteazoiu Streptomyces griseus

The ariticle deals with gelatin hydrolysis by the crystalline preparation of the Str. griseus protease. 12.1% of 1080 peptide bonds available in 105 g of protein split for 24 h at 40 C. The bonds of 8-9 types which involve N-end of glycine, serine, phenylalanine, threonine, leucine, valine, glutaminic acid, lysine break at once. The process occurs with delay, and 0.25, 0.5, 6 and 24 h after there occurs a breakage of the 42d, 61st, 117th and131st bonds. The middle size of the peptide chain of the initial protein is 604 amino acid residues, in the hydrolyzate 30, 22, 11.6 and 11.3 residues are found within these intervals, respectively. Main changes occur in the fraction of soluble peptides where number of N-terminal amino acids rises from 25 to 80. Some data are obtained on the total specificity of the Str. griseus protease. It splits mostly the bonds which involve the N-end of glycine (51%), alanine 2%), serine (9%). The content of the definite amino acid in gelatin shows that hydrolysis bonds of serine and threonine accounts for 35.2 and 35.6%, valine and leucine for 23.6 and 24.7%, glycine and alanine for 18.8 and 13%, methionine, lysine, glutaminic and asparagic acids for 7-9%; the proline bonds are not splitted at all. An assumption is advanced on the presence of four groups of bonds in gelatin; the rate of their hydrolysis corresponding to the enzyme specificity. The Str. griseus protease splits as free amino acids 10 mol of serine of 35,5, 5.5 mol of leucine of 26.3, 3.6 mol of threonine of 19.8 and only 4 mol of glycine of 363 available in gelatin.