Enzymatic properties of neuraminidase from corynebacterium diptherial

Enzymatic properties of neuraminidase isolated from non-toxigenic strain C7 of diphteritic bacteria are studied. The enzyme has the pH optimum 5.5--6.0 in acetate buffer and the temperature optimum 38 degrees C. Neuraminidase has the highest substrate affinity to glycoproteins of equine blood serum, the lowest affinity--to 3-N-acetylneuraminosyllactose and ovomucin. The Km values was 4.3-10(-4) at optimal conditions under the hydrolysis of 3-N-acetylneuraminosyllactose, Vm was 0.05+/-0.02 muM NANA/hour/mg of protein. The following esters of N-glyconoyl-glycine were shown to be competitive inhibitors of neuraminidase: 1) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-arabinooctonic acid; 2) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-glucoheptodecanic acid; 3) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-galactonic acid; 4) methyl ester of 3-aza-4-oxo-2,3,4-trideoxy-D-gluconic acid, Ki values being 6.5-10(-4), 4.5-10(-4); 9.5-10(-4) and 7.1-(10-3) M, respectively.     

Distribution of histocompatibility antigens in patients with pulmonary tuberculosis depending on disease course and immune response pattern

In mature male rabbits and outbred male rats (body weight 180-280 g) the implantation of the different tissues (adenohypophysis, ventricular myocardium, pharyngeal and bronchial epithelium) with hypothalamic nonapeptidergic nuclei in vivo and in vitro was performed by means of light microscopy, histochemistry, immunocytochemistry, histoautoradiographic (3H Thymidine) and electron microscopy methodics. It is demonstrated that hypothalamic nonapeptides (oxytocin and vasopressin) and monoamines are the interlevel regulatory factors of the proliferation, growth and cytodifferentiation of the different genesis tissues. Their role in realization by tissues of histo- and organotypic potentiality adaptive properties and adequate intercellular correlations in appropriate histotypes is indicated.     

Penetration of antibiotics into experimental foci of inflammation under the influence of proteolytic enzymes

The effect of trypsin or chemotrypsin on the levels of benzylpenicillin, ampicillin, oxacillin, kanamycin or tetracycline in the peritoneal inflammation fluid, as well as the effect of trypsin on penetration of these antibiotics into the granulemas of 2 types was studied. It was found that intramuscular administration of the enzymes to animals in a dose of 10 mg/kg resulted in increased levels of penicillins and kanamycin in the inflammation peritoneal fluid. An analogous effect of trypsin was observed with respect to experimental granulemas. The levels of tetracycline in restricted inflammatory foci increased only after intraperitoneal administration of trypsin to rats. Increased penetration of benzylpenicillin into the peritoneal fluid and connective tissue granulema under the effect of the enzymes was observed. The effect of trypsin on penetration of benzylpenicillin into granulema according to Selie did not differ from the effect of the enzyme on penetration of semisynthetic penicillins and kanamycin into it.     

Effect of retinol deficiency on the activity of phospholipase A lysosomal enzymes in rat testes

In the testes homogenates of rats kept on a A-deficient ration and receiving additionally retinyl-acetate (control) and retinoic acid (experiment) the activity of the phospholipases A1 and A2, with 1-acyl-2(1-14C)-oleoyl-SN-glycero-3-galactosidase and acid phosphatase employed as a substrate, was investigated. In the testes of rats receiving retinyl-acetate the activity of the phospholipases A1 and A2 was greatly declining. An addition of retinyl to the testes homogenates of test rats contributed to re-establishing the activity of the phospholipases up to the control level. In the testes of rats receiving retinoic acid a reduced activity of the acid phosphatase and a rise of beta-galactosidase, as compared to their activity in controls was also demonstrable.