TY - JOUR
T1 - Proteolytic specificity of plasmin on bovine αs1-casein
AU - McSweeney, P. L.H.
AU - Olson, N. F.
AU - Fox, P. F.
AU - Healy, A.
AU - Hϕjrup, P.
PY - 1993/7/1
Y1 - 1993/7/1
N2 - The proteolytic specificity of plasmin (fibrinolysin, E. C. 3.4.21.7, from bovine plasma) on bovine αs1-casein was determined in solution in 50 mM ammonium bicarbonate buffer, pH 8.4, at 37°C. Peptides, isolated by reverse-phase high performance liquid chromatography on a C18 column or by electroblotting from urea-polyacrylamide gel electrophoretograms, were identified from their amino acid sequence and mass. The principal plasmin cleavage sites were found at Arg22-Phe23, Arg90-Tyr91, Lysi102-Lys103, Lys103-Tyr104, Lys105-Val106, Lys124-Glu125and Arg151-Gln152. The initial cleavage sites and the order of production of small (pH 4.6-soluble) peptides suggest that αs1-casein was cleaved initially towards the centre of the molecule.
AB - The proteolytic specificity of plasmin (fibrinolysin, E. C. 3.4.21.7, from bovine plasma) on bovine αs1-casein was determined in solution in 50 mM ammonium bicarbonate buffer, pH 8.4, at 37°C. Peptides, isolated by reverse-phase high performance liquid chromatography on a C18 column or by electroblotting from urea-polyacrylamide gel electrophoretograms, were identified from their amino acid sequence and mass. The principal plasmin cleavage sites were found at Arg22-Phe23, Arg90-Tyr91, Lysi102-Lys103, Lys103-Tyr104, Lys105-Val106, Lys124-Glu125and Arg151-Gln152. The initial cleavage sites and the order of production of small (pH 4.6-soluble) peptides suggest that αs1-casein was cleaved initially towards the centre of the molecule.
UR - https://www.scopus.com/pages/publications/0027840961
U2 - 10.1080/08905439309549853
DO - 10.1080/08905439309549853
M3 - Article
AN - SCOPUS:0027840961
SN - 0890-5436
VL - 7
SP - 143
EP - 158
JO - Food Biotechnology
JF - Food Biotechnology
IS - 2
ER -