Fragmentation of Bovine Serum Albumin by Proteolytic Enzymes

Fragmentation of Bovine Serum Albumin by Proteolytic Enzymes 

At pH 3 the product from peptic hydrolysis of BSA was complex (Weber and Young, 9Ma,b Peters and Hawn, 1%7 Pearlman and Fong, 

Commercially available BSA has been found to vary in its susceptibility to tryptic digestion (King and Spencer, 1970 Habeeb, 1977u). Some batches were resistant to trypsin, and the susceptibility to tryptic digestion paralleled the availability of disulfide bonds to reduction in the 

25 C b. 29,000 c. 34,000 Amino acid composition of b and c was identical but differed from that of a 

All fragments were pure with no internal scissions fragments 5 and 6 are derived from adjacent regions at the NH -terminal half similarly, fragments 3 and 4 are derived from the COOH-terminal half 

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D. Fragmentation of Bovine Serum Albumin by Proteolytic Enzymes... 

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