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Biomedical subjects

M P Chernikov

Publications and source records attributed to M P Chernikov.

At least 19 recordsLinked to original sources
PubMed1987

[The role of the adenylate cyclase system in the inhibition of gastric secretion by products of limited hydrolysis of kappa-casein].

The influence of the peptide inhibiting gastric acid secretion and derived from kappa-casein on the levels of cAMP, cGMP and adenylate cyclase activity of rat gastric mucosa was studied. Intravenous peptide preparation administration failed to alter cyclic nucleotide levels. The revealed decrease of adenylate cyclase activity was due to the presence of calcium in the investigated peptide preparation. It was assumed that cyclase system of the rat gastric mucosa cells were not involved in the inhibition of gastric acid secretion by the peptide preparations under study.

Adenylyl Cyclases↗
PubMed1986

[Proteolysis of blood plasma proteins in the stomach in early ontogeny].

Proteolysis of milk substitutes containing fibrinogen, casecid and bovine serum albumin as protein components was studied. Artificial feeding of newborn rats has shown high casecid and fibrinogen utilization. Casecid and fibrinogen contained in milk substitutes delayed protein evacuation from the stomach, while bovine serum albumin intensified protein evacuation. Adaptive changes in enzyme-forming gastric function depend on the protein quality.

Animals↗
PubMed1986

[Mechanism of inhibition of acid secretion into the stomach by peptides of kappa-casein].

The inhibitory effect of peptides formed in a reaction of limited proteolysis on stimulated gastric acid secretion was studied in rats as well as the changes of gastrin level in the blood serum and antral gastric mucosa. The acid secretion decreased after intraluminal administration of the peptide by 51% in the rat isolated stomach, and gastrin level decreased by 8.3% in the blood serum. The mechanism of action of peptide derived from K-casein was discussed.

Animals↗
PubMed1985

[Lysosomal proteinase activity and the the lysosomes of the small intestine in postnatal ontogeny].

It has been shown that in postnatal animals, the activity of lysosomal proteinases in the distal part of the small intestine was considerably higher than in the proximal one. With transition from milk to definitive nutrition, the activity of lysosomal proteinases gets equalized in the proximal and distal parts of the small intestine. The data concerning the proximo-distal gradient of distribution of the activity of lysosomal proteinases have been supported. Transition from milk to definitive nutrition has given rise to ultrastructural alterations in the lysosomal apparatus.

Acid Phosphatase↗
PubMed1985

[Hormonal regulation of anabolic processes and of protein utilization efficiency in the early postnatal period].

The levels of thyroid, pituitary and steroid hormones-thyroxine, triiodothyronine and 11-hydroxycorticosteroids in the blood serum, somatotropin in the pituitary, and processes of protein assimilation were studied in rats in the early postnatal period. The highest endogenous production of thyroxine, triiodothyronine and somatotropin was detected in 15-day-old rats. The highest level of protein utilization was detected in 7 to 15-day-old rats, followed by the lowering of the utilization on changing over to definitive nutrition. Endogenous production of the anabolic hormones thyroxine, triiodothyronine and somatotropin was found to correlate with a high level of protein utilization in rats within the first days of life after birth.

11-Hydroxycorticosteroids↗
PubMed1984

[Proteolysis of milk proteins in young children].

Distinct pancreatic activity was observed in duodenal chyme of newly born children. Rapid evacuation of protein from stomach was noted in artificial feeding. The tryptic activity was increased in duodenal contents after the introduction of artificial feeding. Amino acids were mainly liberated in the course of cavitary digestion of proteins. Some of the amino acids (cysteine, phenylalanine) were absorbed in a bound form.

Amino Acids↗
PubMed1983

[Effect of kappa-casein glycomacropeptide on gastrointestinal motility in dogs].

Glycomacropeptide, which provoked a significant inhibition of food motility of the stomach fundus on intravenous injection to dogs in a dose of 10 mg, was isolated from the products of restricted pepsin proteolysis of cow kappa-casein with the aid of gel chromatography on Sephadex G-25 and G-10. Glycomacropeptide administered on an empty stomach produced cyclic-repetitive vomiting. Physiological action of glycomacropeptide (inhibition of gastric secretion and motility) may play an important role in the preservation of biologically active milk proteins and peptides in the gastrointestinal tract of the newborn.

Animals↗
PubMed1982

[In vivo formation from rat milk proteins of a peptide inhibitor of gastric secretion].

A peptide fraction was isolated from the gastric content of 10-day-old suckling rats by Sephadex G-25 and G-10 chromatography. Intravenous injection of peptide (15 mg) had a powerful inhibitory action on gastric secretion of dogs with Pavlov pouches. It is assumed that this fraction is formed from rat casein and inhibits gastric secretion in the newborn, reducing rat milk proteolysis.

Animals↗
PubMed1979

[Milk protein digestion and lysosomal proteinases of the ileal mucosa in young rats].

The proteolytic activity of lysosomal and pancreatic proteinases was studied in the chyme and tissue homogenates of the jejunum and ileum of 12- and 30-day rats in order to elucidate whether lysosomal proteinases of the mucous membrane of the ileum participate in cavitary digestion. During milk feeding the proteolytic activity of acid (lysosomal) proteinases in the ileum was 3 times greater than in the jejunum, which has been demonstrated both for the mucous membrane and the contents of these parts of the small intestine. In rats on definitive nutrition the activity of acid proteinases from the jejunum and ileum remained almost unchanged both in the mucous membrane and in the contents. The data obtained also indicate that pancreatic proteinase absorbed from the chyme of the small intestine may participate in parietal digestion.

Animals↗