Specificity of milk-clotting enzymes towards bovine kappa-casein.
Limited proteolysis of bovine kappa-casein has been investigated with porcine pepsin A and C, and with the 2 microbial proteinases Mucor miehei proteinase and Endothia parasitica proteinase. The liberated C-terminal glycomacropeptide of kappa-casein was isolated after precipitation in 3% trichloroacetic acid followed by high-performance gel-permeation chromatography on a TSK G3000 SW column. From amino acid analyses and N-terminal sequencing of the liberated peptide it is concluded that porcine pepsin A, C and Mucor miehei proteinase cleave the same bond as chymosin: Phe-105-Met-106 whereas Endothia parasitica proteinase cleaves the bond Ser-104-Phe-105.
Drøhse
H B
HB
Institute of Biochemical Genetics, University of Copenhagen, Denmark.
Foltmann
B
B
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000302:isolation & purification; D000818:Animals; D002364:Caseins / Q000378:metabolism*; D002417:Cattle; D012085:Chymosin; D010450:Endopeptidases; D006020:Glycopeptides / Q000378:metabolism*; D008892:Milk / Q000201:enzymology* / Q000502:physiology; D008969:Molecular Sequence Data; D009584:Nitrogen; D010434:Pepsin A; D012697:Serine Endopeptidases; D013379:Substrate Specificity
D000596:Amino Acids; D002364:Caseins; D006020:Glycopeptides; C020251:kappa-casein glycomacropeptide; D010450:Endopeptidases; D012697:Serine Endopeptidases; C032923:microbial serine proteinases; D010434:Pepsin A; D012085:Chymosin; D009584:Nitrogen