| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10536857 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2012 | 8 Pages |
Abstract
⺠Importance of kringle domains 4 and 5 in substrate plasminogen activation is shown. ⺠Selective kringle truncations show increase of nearly two orders of magnitude in catalysis. ⺠Kringle-swapping experiments were done between PG kringles and those of tPA and uPA. ⺠A subtle conformational trait in the substrate kringles appears to be decisive during catalysis by SK.HPN. ⺠This study reveals a novel, substrate-driven mechanism of action for streptokinase.
Keywords
SDSDEAE-SepharoseEACAuPAHPNSTIHuman plasminogenHPGPAGEIBSNPGBtPAIPTGp-nitrophenyl p-guanidinobenzoateisopropyl-1-thio-β-d-galactopyranosideKcatε-aminocaproic acidstaphylokinasestreptokinasepolyacrylamide gel electrophoresissodium dodecyl sulfateFibrinolytic systemCatalysistissue plasminogen activatorplasminogen activatorurokinase plasminogen activatorInclusion bodiessoybean trypsin inhibitorPlasminogenPichia pastorisSak
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Kishore K. Joshi, Jagpreet S. Nanda, Prakash Kumar, Girish Sahni,