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Biomedical subjects

V Ia Cherniak

Publications and source records attributed to V Ia Cherniak.

9 recordsLinked to original sources
PubMed1990

[Characteristics of immune complexes in myocardial infarct].

Nonspecific circulating immune complexes (CIC), different in size and stability, are detectable in the blood sera of patients with myocardial infarction; changed concentration of these complexes appears to be a reflection of the defense response of the body, aimed at homeostasis maintenance. No relationship between cardiac glycosides and CIC levels was revealed in patients with myocardial infarction. A reduction of the level of 'large' CICs by days 21-30 of the condition was observed in the patients treated with anticoagulants from the first day of the disease. A low CIC level in the acute period of the disease is a prognostically unfavorable sign in respect of the outcome of the condition.

Anticoagulants↗
PubMed1989

[Dissociation of hexamers of cytochrome P-450 LM2 in the presence of the non-ionic detergent emulgin 913].

It was shown that the maximal degree of dissociation of cytochrome P-450 LM2 hexamers in the presence of the nonionic detergent Emulgene 913 (20 degrees C) is observed at the detergent concentration of about 0.2%. Using equilibrium centrifugation in solutions of different density, the molecular mass of the dissociation product minus that of the bound detergent was found to be equal to 50 +/- 8 kDa, thus corresponding to the molecular mass of the monomer. One cytochrome P-450 LM 2 molecule binds 80 +/- 20 molecules of Emulgene 913.

Centrifugation↗
PubMed1978

[Interaction of protein inhibitor from potato (protein with pI 7.3) with proteinases].

The interaction between protein inhibitor of serine proteinases from potato (protein with pI 7.3) and enzymes was investigated. The main complex present in mixtures of the inhibitor with trypsin, chymotrypsin or subtilisin contained one dimeric inhibitor molecule and one molecule of either enzyme. At high ratio enzyme/inhibitor the complexes were formed which contained more than one bound enzyme molecule. The interaction with enzymes does not include the proteolytic degradation of inhibitor with concomitant lowering of its molecular weight. The inhibitor obtained after the dissociation of inhibitor--chymotrypsin complex, preserve its capacity to form stable complexes with the enzyme.

Chymotrypsin↗
PubMed1976

[Physico-chemical properties of a protein-inhibitor of serine proteinases from the potato].

Serine proteases inhibitor with pl-7.3, isolated from potatoe tubers by isoelectric focusing procedure as described previously (V.V. Mosolov et al., Bioorganic Chem., 1, 1449, 1975), was homogeneous under ultracentrifugation, having sedimentation coefficient S20,w 2.8S. Its molecular weight, investigated by sedimentation equilibrium and gel filtration through Sephadex G-100, was found to be 32500 and 31500 respectively. The Stokes radius R and frictional ratio f/fo were found to be 24 A and 1.14. The molecular weight of the inhibitor as determined by sodium dodecylsulfate polyacrylamide electrophoresis was twice as low as determined in ultracentrifuge and by gel filtration procedure. It is suggested that the inhibitor is dimer and consists of two protomers of equal molecular weight.

Centrifugation, Density Gradient↗
PubMedDate not supplied

[Activation of prothrombin, modified by maleic anhydride, some properties of N-maleyl-thrombin with free alpha-amino groups].

Conditions for the acylation of bovine prothrombin by maleic anhydride are worked out. The reaction is shown to modify not more than 95% of amino groups. The changes in hydrodynamic and electrophoretic properties testify about structural changes of prothrombin as a result of the modification of free amino groups. The activation of maleyl-prothrombin to maleyl-thrombin took place in 25% sodium citrate only in the presence of thrombin and the Xa factor. The increase of modified amino groups in prothrombin resulted in the decrease of the activity of generated maleyi-thrombin. The main fraction of maleyl-thrombin with free alpha-amino groups had a sedimentation coefficient of 2.1 S and possessed a residual esterase activity.

Amines↗