Phosphopeptides derived from hen egg yolk phosvitin: effect of molecular size on the calcium-binding properties.
Two different phosphopeptide (PPP) fragments derived from partially dephosphorylated hen egg yolk phosvitin were prepared by tryptic digestion, and their Ca2+ binding property compared with that of commercial casein phosphopeptides (CPP). The smaller fragment of less than 1 kDa and O-phospho-1-serine did not bind Ca2+ to any significant extend, while PPP of 1-3 kDa showed a higher ability than CPP to render soluble calcium. The results show that not only the phosphoserine residues are critical for Ca2+ binding, but also the molecular size of the phosphopeptides.
Jiang
B
B
Department of Food Science, University of Guelph, Ontario, Canada.
Mine
Y
Y
D000818:Animals; D002118:Calcium / Q000378:metabolism*; D002645:Chickens; D004530:Egg Yolk / Q000737:chemistry*; D005260:Female; D008970:Molecular Weight; D010748:Phosphopeptides / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D010774:Phosvitin / Q000737:chemistry*; D011485:Protein Binding
D010748:Phosphopeptides; D010774:Phosvitin; D002118:Calcium