Phosphopeptides from a Tryptic Hydrolysate of Human Casein.
- 1 January 1961
- journal article
- research article
- Published by Danish Chemical Society in Acta Chemica Scandinavica
- Vol. 15 (7) , 1423-1428
- https://doi.org/10.3891/acta.chem.scand.15-1423
Abstract
Phosphopeptides have been isolated by anion exchange chromatography from a tryptic hydrolysate of human casein. The homogeneity of the phosphopeptide with the highest phosphorus content has been demonstrated and its amino acid composition and terminal amino acid residues determined. It contains 19 amino acid residues and 5 phosphate groups and appears to have the composition Arg[Thr2, Ser5, Glu5, Ileu3, Leu, (PO4)5]Tyr, Lys one of the glutamic acid residues possibly being in amide form.This publication has 3 references indexed in Scilit:
- Gel filtration of tryptic hydrolysates of α-caseinBiochimica et Biophysica Acta, 1961
- THE DETERMINATION OF PHOSPHORUS AND PHOSPHATASE WITH N-PHENYL-p-PHENYLENEDIAMINEJournal of Biological Chemistry, 1957
- The amino-acid sequence in the glycyl chain of insulin. 1. The identification of lower peptides from partial hydrolysatesBiochemical Journal, 1953