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M V Polosatov

Publications and source records attributed to M V Polosatov.

At least 19 recordsLinked to original sources
PubMed1989

[Opioid peptides, regulators of acetylcholinesterase activity].

Studies have been made on the opioid peptides--enkephalins their fragments, and alpha- and gamma-endorphins with concentrations of 10(-8)-10(-4) M, on acetylcholinesterase of human blood erythrocytes. It was found out that these peptides, which were fragments of one propeptide beta-LPH were reversible effectors of acetylcholinesterase. Enkephalins and a number of their fragments were noncompetitive inhibitors. It was shown that natural pentapeptide has the highest inhibitor activity; decreasing of inhibitor activity or the absence of it was a result of pentapeptide molecules degradation. Short endorphins were noncompetitive activators of acetylcholinesterase.

Acetylcholinesterase↗
PubMed1988

[The nature of serum factor precipitating autologous alpha-globulins in rabbits].

The nature of serum factor, resulted from the immune response to human albumin being a precipitant of auto-alpha-globulins in rabbits, have been studied. The use of ion exchange, immunoaffinity chromatography and immunoelectrophoresis has shown, that antibodies to human albumin, carrying the binding site to alpha-globulin in antigen-binding fragment are the factor responsible for alpha-globulin precipitation. The synthesis of antibodies cross-reacting to alpha-globulin gives the evidence of the selective derangement of tolerance to one of organism self antigens during the immune response to heterologous antigen.

Alpha-Globulins↗
PubMed1980

Immunofluorescent localization of gamma-glutamyl transferase in rat and bovine tissues.

A distribution of the enzyme in tissue sections was studied by direct fluorescent technique using immunoglobulins from rabbits immunized with the rat and bovine kidney enzyme. For studies rat and bovine sections of kidneys, livers, pancreas, and small intestine were used. Cell distribution of the enzyme by immunofluorescent method was the same as that by the classical histochemical method. No differences in the enzyme distribution were noted when either immunoglobulins anti-heavy form or immunoglobulins anti light form of the enzyme were used. Bovine kidney enzyme coupled to diazotized p-aminobenzoyl-hexamethylenediamine-sepharose is a effective sorbant for affinity chromatography of antibody. Precipitates formed between antibodies and purified rat or bovine gamma-glutamyl transferases preserves over 60% of the initial enzyme activity.

Animals↗
PubMed1979

[Effect of peptide hormones of the gastrointestinal tract on leukocytes].

A single i. m. administration of pentagastrin or secretin changed the amount of lymphoid and myeloid cells in rats and mice. A total decrease of leucocytes is due to decrease of amount of lymphocytes, eosinophiles, and monocytes. Simultaneously the amount of segment-nuclear and relating to stab neutrophiles increased. After pentagastrin administration the amount of rosette-forming T-lymphocytes decreases. The data obtained suggest the effect of gastrin and secretin on the blood-forming and blood-destroying systems of the organism.

Animals↗
PubMed1979

Interaction of synthetic human big gastrin with blood proteins of man and animals.

Radio gel and affin chromatography were used to study big gastrin interaction with blood proteins of man and animals. The experiments showed that big gastrin interacts with serum proteins in vitro. The gastrin-blood protein complex is labile and readily dissociates (T 1/2 = 8--14 min). A more stable complex is found in acidic medium. Ceruloplasmin is one of the blood serum proteins able to interact with big gastrin. The stability of hormone-protein complex, formed by gastrin and ceruloplasmin, is dependent upon hormone concentration. With the addition of C-terminal penta--and octapeptides to labelled hormone, binding increased. It is speculated that formation of labile gastrin-blood protein complexes is necessary for selective gastrin transport from hormone-producing cells to target cells.

Animals↗
PubMed1977

[Gastrin and blood proteins].

With the aid of affinic, ion-exchange- and gel-chromatography, disc- and immunoelectrophoresis, the blood serum of healthy people and animals was shown to contain proteins capable of interaction with gastrin. These proteins form a system including, along with albumins, globulins with electrophoretic mobility of alpha- and gamma-globulins. The immunoglobulins interacting with gastrin are related to the G class. Presence of a number of forms of the labile, spatially organized structural hormonal protein complexes is suggested, which play the functional part of an effective storage and transport of the hormone from the hormone-producing cell to the effector one, and excitation of its membrane's structures. Such overmolecular complexes seem to be easier recognized by the celleffector and to exert a specific action.

Adult↗