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C‐terminal peptide of streptokinase, Met369‐Pro373, is important in plasminogen activation
Author(s) -
Kim Il Chul,
Kim Jang Seong,
Lee Si Hyoung,
Byun Si Myung
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201563
Subject(s) - streptokinase , peptide , chemistry , residue (chemistry) , mutant , c terminus , amino acid residue , plasminogen activator , biochemistry , n terminus , peptide sequence , activator (genetics) , amino acid , microbiology and biotechnology , biology , gene , medicine , endocrinology , myocardial infarction
Streptokinase(SK), a plasminogen activator, is known to have multi‐domain structure. The function of the C‐terminal region of streptokinase was investigated with SK mutants constructed by truncating 26, 33, 37, 40, 41, 46, 47, 70 or 97 amino acid residues from the C‐terminus. The truncated SKs were expressed in E.coli and purified. The 41 residue deletion (SKP373) from the C‐terminus had not effect on the plasminogen activation activity. However, the deletion of 46 amino acid residues (SKP368) resulted in the dramatic reduction of the plasminogen activation efficiency. The result suggests that the C‐terminal peptide from Met369 to Pro373 of SK may play an important role on the plasminogen activation.