Dr. Girish Sahni

Multiple exosites distributed across the three domains of streptokinase co-operate to generate high catalytic rates in the streptokinase-plasmin activator complex. Biochemistry (2013 in Press) (2) First Structural Model of Full-Length Human Tissue-Plasminogen Activator: A Saxs Data-Based Modeling study. J. Phys. Chem. B (2012) 116(1):496-502. (3) Substrate kringle-mediated catalysis by the streptokinase-plasmin activator complex: Critical contribution of kringle-4 revealed by the mutagenesis approaches. Biochem Biophys Acta–Proteins and Prteomics (2012) 1824: 326-333 (4) Identification through combinatorial random and rational mutagenesis of a substrate-interacting exosite in the gamma domain of Streptokinase. J Biol. Chem. (2011)286, 6458,6469. (5) Molecular cloning, expression, purification and characterization of truncated forms of human plasminogen in Pichia pastoris expression system (2010) Process Biochemistry 45, 1251-1260. (6) Probing the primary structural determinants of Streptokinase inter-domain linkers by site-specific substitution and deletion mutagenesis. BBA Proteins and Proteomics (2010) 1804, 1730-1737. (7) Identification of a new exosite involved in catalytic turnover by theStreptokinase-Plasmin activator complex during humanplasminogenactivation (2009) J Biol. Chem. 284, 32642– 32650. (8) Enhanced production of recombinant streptokinase in Escherichia coli using fed-batch culture (2009) Bioresource Technol. 100:4468-74 (9) Role of the 88-97 loop in plasminogen activation by streptokinase probed through site-specific mutagenesis (2008) BBA Prot. & Proteomics. 1784, 1310-1318. (10) Domain truncation studies reveal that the streptokinase plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover (2003) J. Biol Chem. 278, 30569-30577. (11) Involvement of a nine-residue loop of streptokinase in the generation of macromolecular substrate specificity by the activator complex through interaction with substrate kringle domains (2002) J. Biol Chem. 277, 13257-13267. (12) Cloning, characterization, and expression studies in Escherichia coli of growth hormone cDNAs from Indian zebu cattle, reverine buffalo, and beetal goat (2002) Anim Biotechnol. 13, 179-93. (13) Function of the central domain of streptokinase in
substrate plasminogen docking and processing revealed by site-directed mutagenesis (1999) Protein Sci. 8, 2791-2805. (14) Role of the amino-terminal region of streptokinase in the generation of a fully functional plasminogen activator complex probed with synthetic peptides (1998) Protein Sci. 7, 637-648. (15) Mapping of the plasminogen binding site
of streptokinase with short synthetic peptides (1997) Protein Sci. 6, 1284-1292.