A tryptic peptide from beta-casein depresses protein synthesis and degradation and enhances ureogenesis in primary cultures of rat hepatocytes.
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.
Takenaka
A
A
Department of Agricultural Chemistry, Faculty of Agriculture, University of Tokyo, Japan.
Ohishi
Y
Y
Noguchi
T
T
Naito
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002364:Caseins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D002478:Cells, Cultured; D004247:DNA / Q000096:biosynthesis; D005934:Glucagon / Q000494:pharmacology; D007700:Kinetics; D008099:Liver / Q000187:drug effects / Q000378:metabolism; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D011506:Proteins / Q000378:metabolism; D014357:Trypsin; D014508:Urea / Q000378:metabolism*
D002364:Caseins; D010446:Peptide Fragments; D011506:Proteins; D014508:Urea; D004247:DNA; D005934:Glucagon; D014357:Trypsin