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Biomedical subjects

K N Veremeenko

Publications and source records attributed to K N Veremeenko.

89 records · Page 5Linked to original sources
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[Molecular mechanisms of fibrinolysis and perspectives of thrombolytic therapy].

Modern data on biochemistry of fibrinolysis, molecular mechanisms for interaction of plasmin with fibrin and antiplasmins are discussed. Perspectives of thrombolytic therapy are considered. Evidence for selective action of plasmin, bound with alpha 2-macroglobulin, on fibrin offers new opportunities in research on newer effective thrombolytic drugs.

Animals↗
PubMedDate not supplied

[Alpha 2-macroglobulin: structure, properties and physiological role].

The paper is concerned with the results of recent researches devoted to studies of the structure, properties and physiological role of alpha 2-macroglobulin, one of main inhibitors of blood proteolytic enzymes. Data are presented on its primary and quaternary structure, mechanisms of interaction with proteinases. The role of alpha 2-macroglobulin in regulation of the activity of proteinases participating in blood coagulation, fibrinolysis, kininogenesis, immune reactions is shown. Possibilities of its application in medicine are discussed.

Amino Acid Sequence↗
PubMedDate not supplied

[Proteolytic enzymes of leukocytes in human blood].

Hydrolysis of various substrates by proteolytic enzymes from human blood leukocytes was studied. Among the protein substrates used protamine was hydrolyzed at the highest rate. Among the synthetic substrates--N-benzoyl-D,L-arginine ethyl ester was the one hydrolyzed most rapidly. Effect of native inhibitors of proteinases and of bivalent metal ions on the proteolytic activity in leukocytes was also studied. The highest proteolytic activity, estimated by hydrolysis of protamine, was found in lysosomal and microsomal fractions.

Catalysis↗
PubMedDate not supplied

[Proteolytic enzymes in palatine tonsil lymphocytes].

Homogenates and subcellular lymphycyte fractions of human tonsilla palatina contained proteolytic enzymes operating in slightly acidic (pH 3.6) and slightly alkaline (pH 7.5) media. The enzymes hydrolyzed proteins (hemoglobin, protamine sulphate, kininogen) and syntheitc substrates (N-benz-d,1-arg-p-nitroanilide, N-benz-1-arg ethyl ester, hippuryl-1-lys and bradikinin). Data on localization of the proteolytic enzymes in subcellular lymphocyte fractions of human tonsilla were obtained.

Carboxypeptidases↗