[The heterogeneous character of protein modification during substitution of their amino groups. Acylation of alpha-chymotrypsin]. / Geterogennyi kharakter modifikatsii belkov pri zameshchenii ikh aminogrupp. Atsilirovanie al'fa-khimotripsina.

Thin-layer isoelectric focusing of chymotrypsin modified by stepwise acylation with acryloyl chloride or maleic anhydride revealed a high heterogeneity of modification products, with a maximal number of components near 50% of substituted amino groups. Disc electrophoresis failed to establish the products diversity and could not therefore be used for heterogeneity control. The activity of the modified enzyme towards proteins and low molecular weight substrates depended on the modification reagent and correlated with the electrostatic enzyme--substrate interaction. The low hydrolytic activity towards N-acetyl-L-tyrosine p-nitroanilide was due to the increase in the Michaelis constant; the value of the catalytic constant remained unchanged.

[Plasma kinin system indices in diabetes mellitus patients before and after treatment with prodectin]. / Pokazateli kininovoi sistemy plazmy krovi u bol'nykh sakharnym diabetom do i posle lecheniia prodektinom.

Kinin system was investigated in 82 patients suffering from diabetes mellitus of various severity. To make pathogenetically substantiated pharmacological correction of the kinin system activity prodectin--kinin antagonist--was used in these patients. A conclusion was drawn that the blood plasma kinin system was activated in the patients with moderately severe and severe diabetes. The activity of total kallikrein and kininogen became normal against the background of prodectin treatment. The blood plasma kinin system activity was normalized simultaneously with the improvement of the diabetic angiopathies course.