Characterization of phosphopeptide derived from bovine beta-casein: an inhibitor to intra-intestinal precipitation of calcium phosphate.
Casein phosphopeptide (CPP), a highly phosphorylated peptide fragment which inhibits the formation of hydroxyapatite crystal was isolated from pooled ileal contents of rats fed a semi-synthetic diet containing bovine beta-casein. The estimated amino acid sequence of the CPP was shorter than that of the trypsin-digested beta-casein but the core region consisting of consecutive bindings of phosphoserine was fully conserved. A moderate and exchangeable binding to Ca2+ of the CPP molecule well substantiates the high absorbability of calcium from milk and dairy products.
Sato
R
R
Department of Agricultural Chemistry, University of Tokyo, Japan.
Shindo
M
M
Gunshin
H
H
Noguchi
T
T
Naito
H
H
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002130:Calcium Phosphates / Q000378:metabolism*; D002364:Caseins / Q000032:analysis*; D002417:Cattle; D011232:Chemical Precipitation; D007413:Intestinal Mucosa / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis*; D010748:Phosphopeptides / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains
D000596:Amino Acids; D002130:Calcium Phosphates; D002364:Caseins; D010446:Peptide Fragments; D010748:Phosphopeptides; C485828:alpha-tricalcium phosphate; C485830:tetracalcium phosphate; C485838:calcium phosphate, monobasic, anhydrous; C020243:calcium phosphate; C485829:calcium phosphate, dibasic, anhydrous