These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.
Pubmed for Handhelds
PUBMED FOR HANDHELDS
Search MEDLINE/PubMed
Title: C-terminal peptide of streptokinase, Met369-Pro373, is important in plasminogen activation. Author: Kim IC, Kim JS, Lee SH, Byun SM. Journal: Biochem Mol Biol Int; 1996 Nov; 40(5):939-45. PubMed ID: 8955883. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]