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T T Volodina

Publications and source records attributed to T T Volodina.

16 recordsLinked to original sources
PubMed1990

[Pathogenesis of arthrosis deformans of the knee joint].

The authors have studied the biochemical characteristics (type, aminoacid composition, carbohydrate component content) of the collagene proteins in the articular cartilage in normal conditions and in various expression of deforming arthrosis of the knee joint. The results (collagen of the its type formation, disturbances in the aminoacid composition of collagen of the 1st and 2nd types, changes in the carbohydrate component content, accumulation of procollagen of type 2) allowed to suggest that already at the early stages of development of deforming arthrosis there are distortion of synthesis and disturbance in postsynthetic transformations of the collagen proteins of hyaline cartilaginous tissue which lead to disturbances in the structure and in the function of the matrix and progressive degradation of the articular cartilage.

Adolescent↗
PubMedDate not supplied

[Biosynthesis of rat skin collagen under amino acid imbalance].

Protein differing from the normal one by the content of S-S-bonds and by the amount of the carbohydrate component was found in the acid-soluble fraction of skin collagen in rats which were fed the protein-free diet and the protein-free diet with the glycine loading for 3 and 14 days and tryptophan for 1, 2 and 3 days. The result testifies to the fact that under extremal states in the animal skin there occurs the synthesis of collagen the structure of which differs from that in the normal animal skin.

Animals↗
PubMedDate not supplied

[Role of formic acid in transformation of acetic and succinic acids in animal tissues].

Acetic and succinate acids KoA acyl derivatives interacting with formate were displayed to produce alpha-ketoacids--pyruvate and alpha-ketoglutarate. These acids also interact with formate and make pyruvic and malate acids, while alpha-ketoglutarate, evidently, tricarboxy acids. Interaction of formate with acetic and succinate acids inspite of occurring out of the tricarbone cycle increases the latter metabolic functions.

Acetic Acid↗
PubMedDate not supplied

[Collagen from human joint cartilage in deforming arthritis].

Type II collagen of human cartilage has been comparatively studied in norm and at deforming arthrosis. Collagen preparations are characterized by aminoacid composition and electrophoretic mobility in polyacrylamide gel. It is supposed that at deforming arthrosis the degenerative-dystrophic processes in the articular cartilage of man are caused by appearance of procollagen.

Amino Acids↗
PubMedDate not supplied

[Structure and properties of collagen in leukemia].

Collagen I was isolated from human bone tissue and from mice bone tissue of the AKR-50 strain at the pronounced stage of leukosis. Dissimilarity of native and leukemic collagens was exhibited after evaluation of their amino acid composition, electrophoretic mobility in polyacrylamide gel containing SDS, content of the carbohydrate moiety as well as of isopoints, elution profiles in reverse-phase chromatography and gel filtration and electron microscopy of SLS-crystallites. Impairments of collagen processing in leukemia appear to be responsible for its alterations in structure and properties.

Adolescent↗
PubMedDate not supplied

[Type I collagen in rat skin in an excess of dietary amino acids].

Type I collagen in skin of rats who were given redundant amounts of leucin, valine, methionine or phenyl alanine differed essentially from the normal level in the amino acidic composition. Considerable shifts in the value of pI of the proteins under study as compared with the normal level are found during isofocusing. When studying subunits of collagen preparations by the reverse-phase chromatography certain differences typical of each studied state are revealed in the elution profiles in normalcy and under amino acid loadings.

Amino Acids↗
PubMedDate not supplied

[Acid-soluble collagen in the skin of rats who received a tryptophan load and were kept on a protein-free diet].

Crystalline preparations of acid-soluble collagen of rat skin in norm and with tryptophan load against a background of the protein-free diet were fractionated by differential salting out using NaCl in concentrations corresponding to precipitation zones of collagen 1,3 and 4. Amino acid composition, electrophoretic mobility in polyacrylamide gel, profiles of elution from CM-cellulose, content of the carbohydrate component and--S--S-bonds were studied in proteins of the mentioned fractions and in the precipitate insoluble after the pepsin action. Essential differences as compared to the normal level in the amino acid composition and elution profiles were detected in the fraction corresponding to collagen I. Quantitative changes in the carbohydrate component and--S--S-bonds occur due to the fraction inaccessible to the persin action.

Amino Acid Sequence↗
PubMedDate not supplied

[Molecular heterogeneity of collagen in normal and pathologic states].

Collagen, the main protein of the connective tissue, is characterized by considerable heterogeneity. More than five types of collagen molecules, or seven types of subunits coded by different structural genes are studied. Both in the age aspects and under different pathologies the ratio of collagen types in some tissues changes, new types of collagen molecules are synthetized. Collagen not peculiar to the rat skin in normal state is synthetized in the unbalanced nitrogen nutrition with addition of amino acids, such as glycin and tryptophan.

Animals↗
PubMedDate not supplied

[Amino acid composition of preparations acid-soluble skin collagen and free amino acids in rat serum under loading with valine and methionine].

The valine and methionine loading against a background of protein-free diet evokes interrelated changes in amino acid composition of acid-soluble skin collagen preparations and free amino acids pool of blood serum in rats. The isolated collagen preparations also differ essentially from the normal preparations in the content of disulphide groups and elution profiles.

Amino Acids↗
PubMedDate not supplied

[Crystalline preparations of acid-soluble collagen from rat skin].

Crystalline preparations of rat skin acid-soluble collagen are a complex of collagen and glycoprotein of noncollagenic nature. Heat denaturation of the preparation, treatment with urea and DS-Na result in decomposition of this complex. Proteins composing it differ in amino acid composition, the presence of -S-S-bonds, the amount of a carbohydrate component, electrophoretic mobility in polyacrylamide gel and solubility in acid medium. Differential salting out by various NaCl concentrations permits separating the acid-soluble collagen preparations into fractions containing and noncontaining the accompanying noncollagen component. d

Amino Acid Sequence↗
PubMedDate not supplied

[Cartilage collagen in health and in pathology].

The paper deals with the latest data on structure organization of collagen proteins--basic and minor components of the extracellular matrix of the animal cartilage tissue. Their genetic determination and tissue specificity, differences in the initial structure, sizes of spiral and globular domains, availability of --SH- and --S--S-bonds are emphasized. Data are presented which confirm that the change in the collagen state is one of the determining factors in pathogenesis of the cartilage tissue.

Animals↗