The profibrinolytic enzyme subtilisin NAT purified frombacillus subtilis cleaves and inactivates plasminogen activator inhibitor type 1
T Urano, H Ihara, K Umemura, Y Suzuki, M Oike… - Journal of Biological …, 2001 - ASBMB
In this report, we demonstrate an interaction between subtilisin NAT (formerly designated
BSP, or nattokinase), a profibrinolytic serine proteinase from Bacillus subtilis, and
plasminogen activator inhibitor 1 (PAI-1). Subtilisin NAT was purified to homogeneity
(molecular mass, 27.7 kDa) from a saline extract of B. subtilis (natto). Subtilisin NAT
appeared to cleave active recombinant prokaryotic PAI-1 (rpPAI-1) into low molecular weight
fragments. Matrix-assisted laser desorption/ionization in combination with time-of-flight mass …
BSP, or nattokinase), a profibrinolytic serine proteinase from Bacillus subtilis, and
plasminogen activator inhibitor 1 (PAI-1). Subtilisin NAT was purified to homogeneity
(molecular mass, 27.7 kDa) from a saline extract of B. subtilis (natto). Subtilisin NAT
appeared to cleave active recombinant prokaryotic PAI-1 (rpPAI-1) into low molecular weight
fragments. Matrix-assisted laser desorption/ionization in combination with time-of-flight mass …
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