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Fragmentation of proteins by S. aureus strain V8 protease
Author(s) -
Sørensen Steen Bech,
Sørensen Thomas Lykke,
Breddam Klaus
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80667-r
Subject(s) - chemistry , protease , cleavage (geology) , endopeptidase , staphylococcus aureus , ammonium bicarbonate , peptide bond , biochemistry , sodium bicarbonate , phosphate , serine protease , enzyme , stereochemistry , biology , bacteria , organic chemistry , raw material , paleontology , fracture (geology) , genetics
Staphylococcus aureus strain V8 protease is a serine endopeptidase which cleaves peptide bonds at the carboxyl side of Glu and Asp. Specific cleavage at Glu has previously been achieved in ammonium bicarbonate whereas in sodium phosphate cleavage at both Glu and Asp was observed. However, it is shown here that bicarbonate does not restrict the specificity to Glu‐X bonds, it simply inhibits the enzyme. The degradation of a mixture of oxidized insulin and glucagon proceeds similarly in the two buffers, although faster in phosphate.