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Streptokinase contains two independent plasminogen-binding sites.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Streptokinase contains two independent plasminogen-binding sites.
 
Creator Nihalani, D
Sahni, Girish
 
Subject QD Chemistry
 
Description Streptokinase (SK) exerts its thrombolytic effect by activating plasminogen (PG) indirectly, after the formation of an equimolar complex with either PG or plasmin (PN). The location and nature of the PG/PN-binding sites in SK have been explored using limited proteolysis with immobilized trypsin. Employing Western blotting with radiolabeled PG after SDS-PAGE of total tryptic digest, three fragments of MW 7 kD, 19 kD and 31 kD were found to possess PG-binding ability. Each of these fragments was then isolated by reverse phase HPLC and characterised with respect to its sequence, as well as its PG-binding properties by ELISA. These analyses revealed that in addition to a PG-binding site in the region 143-293 reported recently in the literature, there is another distinct, high-affinity and independent PG-binding site, located in the N-terminal region (residues 1-59) of SK. Using a synthetic peptide, the N-terminally located PG-binding-site has been further localised to the region 37-51 of SK. Further, we demonstrate that the PG-binding of this peptide is not mediated through the lysine-binding sites ("Kringles") of PG. This stretch contains a short sequence (LTSRPA) that is also present in the PG-binding domain of human fibronectin.
 
Publisher Elsevier Science/Academic Press
 
Date 1995-12-26
 
Type Article
PeerReviewed
 
Format application/pdf
 
Identifier http://crdd.osdd.net/open/387/1/sahni1995.pdf
Nihalani, D and Sahni, Girish (1995) Streptokinase contains two independent plasminogen-binding sites. Biochemical and biophysical research communications, 217 (3). pp. 1245-54. ISSN 0006-291X
 
Relation http://www.sciencedirect.com/science/article/pii/S0006291X85729026
http://crdd.osdd.net/open/387/