[The thrombocyte-activation factor and endotoxin-induced thrombocyte activation]. / Faktor aktivatsii trombotsitov i éndotoksinindutsirovannaia aktivatsii trombotsitov.

The effect of PAF in aggregation of platelets induced by endotoxin was studied in experiments in vitro. It is indicated that in high concentration (1.10(-7)-1.10(-6) M) PAF did not affect the degree of aggregation of platelets induced by lipopolysaccharides (LPS) S. typhimurium and N. meningitidis. Successive addition to PRP LPS and PAF or joint addition of PAF and LPS did not change the degree of aggregation of each inductor or their sum. A lower concentration of PAF (1.10(-11)-1.10(-9) M) and endotoxin caused a more expressive aggregation of platelets than their successive addition. Stimulating activity of PAF on endotoxin-induced aggregation, perhaps, is caused by involvement of metabolism of arachidonic acid during blood platelets activation.

[Disorders in the thrombocyte link of hemostasis during endotoxinemia and their correction with the inhibitor of prostaglandin biosynthesis, indomethacin]. / Narusheniia v trombotsitarnom zvene gemostaza pri éndotoksinemii i korrektsiia ikh ingibitorom biosinteza prostaglandinov, indometatsinom.

After 10 minutes of endotoxin Salmonella typhimurium (1 mg/kg) injection into rabbits thrombocytopenia appeared, the aggregation and secretory function of circulating platelets reduced, the transformation of platelet forms from disk-shaped into spheroidal took place. On the surface of plasmatic membranes the pseudopodies and aggregates examining samples of PRP were observed. Indomethacin, blockator of biosynthesis of prostaglandins results in normalisation of morphofunctional properties of platelets.

[Monoamine oxidation in the mitochondrial fraction of bovine kidney catalyzed by monoamine oxidase type B]. / Okislenie monoaminov v mitokhondrial'noi fraktsii pochek byka, kataliziruemoe monoaminoksidazoi tipa B.

Oxidative deamination of tyramine, serotonin and benzyl amine in bovine kidney mitochondria was inhibited by low concentrations of deprenil (but not clorgylline). These data and the patterns of the plots of residual enzymatic activity against concentration of the inhibitors as well as the "mixed substrates" experiments suggest occurrence in bovine kidney mitochondria of monoamine oxidase of the B type only, which has to be considered in studies on the nature of monoamine oxidases using bovine kidney mitochondria as a rich source of monoamine oxidase activity.

[Purification and properties of acid alpha-glucosidase (gamma-amylase) from the human liver]. / Ochistka i svoistva kisloi al'fa-gliukozidazy (gamma-amilazy) iz pecheni cheloveka

Acid alpha-glucosidase from human liver was 720-fold purified by means of a specific sorption on Sephadex G-150 and a specific desorption from Sephadex by the competitive inhibitor, methyl-alpha-D-glucopyranoside. The preparation obtained was homogenous in ultracentrifuge and polyacrilamide gel electrophoresis. The enzyme possessed both maltase and glucoamylase activities and splitted maltose, amylopectin and glycogen with Km values of 7mM, 7.7 mg/ml and 5 mg/ml respectively. Methyl-alpha-D-glucopyranoside competitively inhibited the enzymatic hydrolysis of polysaccharides (Ki=6.95 mM) and did not affect the maltose degradation. The sedimentation coefficient of the purified enzyme preparation was 5.4 S; in 5 M guanidine. HCl the coefficient decreased to 2.2 S, which testified to the fact that the enzyme molecule consisted of subunits.