A tryptic peptide from beta-casein depresses protein synthesis and degradation and enhances ureogenesis in primary cultures of rat hepatocytes

A Takenaka; Y Ohishi; T Noguchi; H Naito

doi:10.1016/0020-711x(91)90178-p

A tryptic peptide from beta-casein depresses protein synthesis and degradation and enhances ureogenesis in primary cultures of rat hepatocytes

Int J Biochem. 1991;23(4):483-90. doi: 10.1016/0020-711x(91)90178-p.

Authors

A Takenaka¹, Y Ohishi, T Noguchi, H Naito

Affiliation

¹ Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo, Japan.

PMID: 2015957
DOI: 10.1016/0020-711x(91)90178-p

Abstract

1. A peptide which enhances ureogenesis in primary cultured hepatocytes of rats was isolated from a tryptic digest of bovine beta-casein. 2. The structure of the peptide was Ala-Val-Pro-Tyr-Pro-Gln-Arg which is located from 177th to 183rd residues from N-terminal of beta-casein. 3. The peptide also showed the activity to inhibit protein synthesis and protein degradation. 4. It also inhibited DNA synthesis of hepatocytes induced by insulin and/or epidermal growth factor.

MeSH terms

Amino Acid Sequence
Animals
Caseins / chemistry
Caseins / isolation & purification
Caseins / pharmacology*
Cells, Cultured
DNA / biosynthesis
Glucagon / pharmacology
Kinetics
Liver / drug effects
Liver / metabolism
Molecular Sequence Data
Peptide Fragments / chemistry
Peptide Fragments / isolation & purification
Peptide Fragments / pharmacology*
Proteins / metabolism
Trypsin
Urea / metabolism*

Substances

Caseins
Peptide Fragments
Proteins
Urea
DNA
Glucagon
Trypsin