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Biomedical subjects

A A Sinichkin

Publications and source records attributed to A A Sinichkin.

16 recordsLinked to original sources
PubMed2002

[Identification of cysteine-containing proteins following separation by disk electrophoresis].

Several approaches to measurements of cysteine-containing proteins are known. These proteins are essential for normal function of cells, tissues, organs, and the total organism under natural conditions and during exposure to exo- and endogenic pathological factors. Unfortunately, the routine methods are inconvenient and have many drawbacks, which impedes their wide use. The authors suggest a simple, cheap, and rapid method for identification of cysteine-containing proteins after their separation by disk electrophoresis in polyacrylamide gel.

Cysteine↗
PubMed1998

[Effect of albumin on the Na, K-ATPase activity in the rat erythrocytes during immobilization stress].

Immobilisation stress (IMS) led to a 42% decrease in erythrocyte Na, K-ATPase activity in rats. Pre-treatment of the "stressed" erythrocytes with human serum albumin (HSA) and 1-day exposition of the HSA prior to the IMS led to stabilising of enzyme activity at the control level. Absence of inhibiting effect of non-protein supernatants of the blood plasma of stressed rats on enzyme activity of normal erythrocytes was shown in presence of the HSA both in vitro and in vivo. The mechanism of the HSA protective effect on the Na,K-ATPase activity of erythrocytes in the IMS, is discussed.

Animals↗
PubMed1979

[Study of bromthymol blue-prealbumin in the blood serum of rats under hyperbaric oxygenation].

Three-fold increase of BTB-prealbumin (Rm 1.0) in rat serum following fierse convulsions under hyperbaric oxygenation (6 ati, 30-35 min) has been proved by disc electrophoresis. Glial S100-protein and 7-fold increase in the all-organ component of brain BTB-prealbumin were found by immunochemistry to appear in the serum of experimental rats. The consequences of disorders in the blood-brain barrier for non-specific, all-organ proteins and potentialities of protein output from the brain into the blood similarly to neurophysins under hyperbaric oxygenation are discussed.

Animals↗
PubMed1977

[Investigation of rat brain prealbumins].

12 prealbumines of rat brain water-soluble fraction were studied. Neither lipid components nor carbohydrate ones were found out in the proteins. Three of the proteins appeared to be RNA-proteids. Their subcellular distribution was investigated. The effects of temperature, salts, acids and ethanol on disc electrophoretic spectrum of brain prealbumines were closely observed. The amino acid composition, properties, compartmentation, tissue and species specificity of one of the prealbumines were studied in detail. The protein is marked as BTB-protein, as it migrates under disc electrophoresis in 7,5% polyacrylamide gel with the "witness" front of bromothemol blue (BTB). The content of BTB-protein is 0.06--0.08 gr per 100 gr of wet tissue. The protein is RNA-proteid. Its molecular weight is 10,000--20,000. BTB-protein contains 42 mole % of acidic amino acids and 5.4 mole % of alkaline ones. The protein was found in nuclear and cytoplasmic fractions. It is mainly an all-organs protein. Small amount of this protein is found in blood serum. BTB-protein can be found on the disc electrophoregramms of embryo and newborn rats brain proteins, as well as of the brain of other mammals, birds and amphibia. BTB-protein is resistant to boiling and to the effects of salts, acids, ethanol. It is suggested that BTB-protein has heterogenous structure and may be of neurophysin nature.

Amino Acids↗
PubMed1977

[The problem of structural heterogeneity of brain prealbumin].

The investigation of structural heterogeneity of rat brain prealbumine (BTB-protein) has been carried out. BTB-protein migrates in disc electrophoresis in 7.5% and 10% polyacrylamide gel with the "witness" front of bromthemol blue (BTB). The protein dissociated in three components in 8M urea. Three components with the molecular weight 14500, 8000 and 6900 daltones were found by disc electrophoresis of BTB-protein in 0.1% SDS-Na. Glycine was shown to be N-terminal amino acid of this BTB-protein complex.

Animals↗
PubMedDate not supplied

[Effect of carbohydrates and polyols on amide content and protein fragmentation in a lactoglobulin preparation].

Certain carbohydrates and polyols are used at various stages of the production of immunobiological preparations as stabilizers of biological activity, particularly in the production of lactoglobulin (against opportunistic pathogens) using membrane ultrafiltration. This study concerns the effect of these substances on changes in the amide content in proteins of this lactoglobulin. Lactoglobulin was incubated in near-physiological (0.9% NaCl, pH 5.5) 10% solutions of glucose, fructose, and sorbitol at 4 and 35 degrees C for 7, 14, and 28 days. A lactoglobulin solution in 0.9% NaCl, pH 5.5, was used as the control. All substances studied suppressed the reduction of the amide group content of asparagine and, in contrast, increased the rate of amide group removal from glutamine residues in proteins of lactoglobulin preparations.

Amides↗
PubMedDate not supplied

[Correction of the immunologic shifts induced by hemosorption in sepsis of the newborn].

Alongside with a positive clinical effect, hemosorption (HS) leads to the elimination of humoral immunity factors (Ig, FN) from the blood, having no effect on the phagocytic activity of leukocytes. Massive immunocorrection in doses 2-3 times higher than the age-matched ones, increases considerably the levels of IgG and FN. Immunomodulating effect of HS is enhanced when HS is combined with ultraviolet blood irradiation.

Bacterial Infections↗
PubMedDate not supplied

[Brain prealbumins].

The paper generalizes the results of research concerned with structural heterogeneity of the nervous system prealbumins, their posttranslation modifications, interactions and complexing with low- and high-molecular compounds as well as of individual prealbumins of the nervous tissue, their dynamic state in the brain-blood-cerebrospinal fluid system.

Animals↗
PubMedDate not supplied

[Effect of hyperoxia on RNA and protein concentration in cortical and spinal motor neurons and surrounding neuroglia].

Double-beam recording visible cytospectrophotometry showed that 30-minute convulsions due to 6 at. ga. hyperoxia result in a decrease in the RNA and protein content per cell in layer V neurons of the cerebral motor cortex and in the motoneurons of spinal cord anterior horn in albino rats. A decrease is also found in the glial cells, except for a spinal cord neuroglia. A decrease in the RNA content in the neurons as well as the protein content in the neurons and glia of the spinal cord is more pronounced than in similar structures of the cerebral motor cortex. The quantity of RNA and protein in the neurons and neuroglia of the cerebral cortex remins decreased for 24 h after hyperoxia cessation. In the spinal cord motoneurons the level of the RNA and protein becomes normal 3 h after hyperoxia, and 24 h later it exceeds the initial one.

Animals↗
PubMedDate not supplied

[Structural heterogeneity of prealbumin fraction rat brain].

Biochemical and immunochemical studies were carried out to prove the structural heterogeneous and supermolecular nature of the rat brain BTB-protein. Microheterogeneity of the BTB-protein--6 subfractions--was found by disc electrophoresis in 30% gel and isoelectric focusing (pH 3-5). Two of the proteins are RNA-proteids. The presence of neurophysin in BTB-protein is suggested. Heterogeneity of BTB-protein according to its antigenic specificity was found by methods of immunodiffusion, immunoelectrophoresis and immunodisc electrophoresis. Heterofunctional complexes are supposed to exist in the nervous tissue which possesses various structural qualities and functional activities within the complex.

Animals↗