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A A Zamiatnin

Publications and source records attributed to A A Zamiatnin.

11 recordsLinked to original sources
PubMed1992

[The general functional characteristics of endogenous regulatory oligopeptides].

A number of physicochemical factors of the endogenous regulatory oligopeptides are considered to be the basis of their general functional properties as indicated by the phenomena of cascade regulation, morphogenesis, behaviour and biological evolution. Functional characteristics and chemical features of classical transmitters and, probably, other endogenous substances allow to consider them as the integrity of endogenous molecular regulators.

Animals↗
PubMed1992

[The place of carnosine among physiologically active peptides].

The results of analysis of EROP-Moscow data base concerning structural and functional peculiarities of endogenous regulatory oligopeptides are reviewed in relation to carnosine, the first endogenous peptide bioregulator. The dipeptide fragment ala-his is widely distributed in natural systems, in particular in various representatives of living organisms. The main structural peculiarity of carnosine is its elongated "filamentous" structure with a positively charged N-terminus and a cyclic radical characteristic of large physiologically active oligopeptides. The relatedness of carnosine to other oligopeptides also becomes apparent during the analysis of its role in various regulatory systems of the body.

Carnosine↗
PubMed1989

[The system of natural physiologically active peptides].

The system of natural physiologically (endocrino-, immuno-) active peptides was shown to have a special amino acid content of peptides as the basis of their polyfunctionality, and the amino acid sequence as the basis of the specificity. The approach to the quantitative definition of oligopeptides was based on a notation system and made it possible to study the correlation between the structure and the activity. The findings can be used for the synthesis of new active peptide compounds.

Amino Acid Sequence↗
PubMedDate not supplied

[Endogenous regulatory oligopeptides: their structure, functions and localization].

A number of problems connected with the study of several hundreds of known endogenous peptide molecules have been considered on the basis of data obtained from EROP-Moscow database. A large number of peptide structures can be reduced to a relatively small number of peptide families formed on the basis of homology of amino acid sequence. The ability of most peptides to participate in different regulatory systems of an organism has been demonstrated and the physical and chemical basis for specificity and ambiguity has been discussed. Most problems of structure, function, and localization of endogenous regulatory peptides are similar both in higher and in lower organisms.

Amino Acid Sequence↗
PubMedDate not supplied

[Physico-chemical characteristics of endogenous regulatory oligopeptides].

Analysis of amino acid residue content in endogenous regulatory oligopeptides possessing a preset spectrum of functional activity has been made. It has been shown that compared to proteins the oligopeptides contain a greater number of positively charged and cyclic radicals. All 525 oligopeptides with the preset spectrum of functional activity contained in EROP-Moscow data bank were found to have the same physicochemical characteristics.

Amino Acids↗
PubMedDate not supplied

[Common physicochemical characteristics of endogenous hormones-- liberins and statins].

The common chemical features of oligopeptide releasing-hormones and release inhibiting hormones were investigated with the aid of computer methods. 339 regulatory molecules of such type have been extracted out of data from computer bank EROP-Moscow. They contain from 2 to 47 amino acid residues and their sequences include short sites, which play apparently a decisive role in realization of interactions with the receptors. The analysis of chemical radicals shows that all liberins and statins contain positively charged group and cyclic radical of some amino acids or hydrophobic group. Results of this study indicate that the most chemical radicals of hormones are open for the interaction with potential receptors of target-cells. The mechanism of hormone ligand and receptors binding and conceivable role of amino acid and neurotransmitter radicals in hormonal properties of liberins and statins is discussed.

Amino Acid Sequence↗