1979PubMedRequires access

[Trypsin and chymotrypsin activity during early postnatal development in the rat].

Chernikov Mp, Nikolaevskaia Vr, E Ia Stan

Open publisher page 0 citations

Abstract

Activities of trypsin and chymotrypsin were studied in pancreas as well as in chyme from three departments of small intestine of rats of various age. Distinct decrease in content of chymotrypsinogen and increase in content of trypsinogen were observed in pancreas at first four days of rat life. In pancreas content of trypsinogen and chymotrypsinogen was as high in 4--20 days old rats as that one in 30-days old animals, maintained at definitive diet. Activity of trypsin and chymotrypsin was the same in duodenal contents of rats of both these groups. Activity of pancreatic proteinases was almost unaltered in chyme of jejunum intestine within first 20 days of life; it was twice increased to 30-days age. Trypsin and chymotrypsin were distinctly activated in chyme of ileum intestine with ageing. The highest activity of pancreatic proteinases was observed in chyme of ileum intestine. The data obtained suggest that rather intensive cavitary digestion of milk protein occurs in newborn rats.

About this research paper

What this paper is about

Activities of trypsin and chymotrypsin were studied in pancreas as well as in chyme from three departments of small intestine of rats of various age. Distinct decrease in content of chymotrypsinogen and increase in content of trypsinogen were observed in pancreas at first four days of rat life. In pancreas content of trypsinogen and chymotrypsinogen was as high in 4--20 days old rats as that one in 30-days old animals, maintained at definitive diet. Activity of trypsin and chymotrypsin was the same in duodenal contents of rats of both these groups. Activity of pancreatic proteinases was almost unaltered in chyme of jejunum intestine within first 20 days of life; it was twice increased to 30-days age. Trypsin and chymotrypsin were distinctly activated in chyme of ileum intestine with ageing. The highest activity of pancreatic proteinases was observed in chyme of ileum intestine. The data obtained suggest that rather intensive cavitary digestion of milk protein occurs in newborn rats.

Why it matters

A significance statement is not available in the OpenAlex record.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

Activities of trypsin and chymotrypsin were studied in pancreas as well as in chyme from three departments of small intestine of rats of various age. Distinct decrease in content of chymotrypsinogen and increase in content of trypsinogen were observed in pancreas at first four days of rat life. In pancreas content of trypsinogen and chymotrypsinogen was as high in 4--20 days old rats as that one in 30-days old animals, maintained at definitive diet. Activity of trypsin and chymotrypsin was the same in duodenal contents of rats of both these groups. Activity of pancreatic proteinases was almost unaltered in chyme of jejunum intestine within first 20 days of life; it was twice increased to 30-days age. Trypsin and chymotrypsin were distinctly activated in chyme of ileum intestine with ageing. The highest activity of pancreatic proteinases was observed in chyme of ileum intestine. The data obtained suggest that rather intensive cavitary digestion of milk protein occurs in newborn rats.

Key concepts: Trypsinogen, Chymotrypsinogen, Chymotrypsin, Trypsin, Internal medicine, Pancreas, Ileum, Endocrinology

Related papers

Back to paper searchBrowse research topicsOriginal source
[Trypsin and chymotrypsin activity during early postnatal development in the rat]. — Research Paper | ScholarLens