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Kwon Gu-Joong Bandi Rajkumar Yang Bong-Suk Park Chan-Woo Han Song-Yi Park Ji-Soo Lee Eun-Ah Kim Nam-Hun Lee Seung-Hwan 《Cellulose (London, England)》2021,28(14):9169-9185
Cellulose - Lignocellulose nanofibrils (LCNFs) were produced from the biomass of Mongolian oak for the first time using deep eutectic solvent pretreatment and mechanical defibrillation. Three... 相似文献
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Bong-Suk Choi Kumar Sapkota Jun-Hui Choi Chang-ho Shin Seung Kim Sung-Jun Kim 《Applied biochemistry and biotechnology》2013,170(3):609-622
Herinase, a new bi-functional fibrinolytic metalloprotease, was purified from a medicinal and edible mushroom Hericium erinaceum. The enzyme was monomeric with a molecular mass of 51 kDa. Analysis of fibrin zymography showed an active band with a similar molecular mass. The N-terminal sequence of herinase VPSSFRTTITDAQLRG was highly distinguished from known fibrinolytic enzymes. Moreover, the enzyme activity was strongly inhibited by EDTA and EGTA, indicating that herinase is a metalloprotease. Herinase exhibited high specificity for the substrate t-PA followed by plasmin. The K m and V max values for H-D-Ile-Pro-Arg-PNA were found to be 4.7 mg and 26.7 U/ml respectively. Similarly, fibrin plate assays revealed that it was able to degrade fibrin clot directly and also able to activate plasminogen. Herinase provoked a rapid degradation of fibrin and fibrinogen α chains and slower degradation of γ chains. It had no activity on the β chains of fibrin and fibrinogen. This result suggests that herinase could possibly contain higher amount of α-fibrinogenase. The activity of herinase was stimulated by metal ions such as Ca2+, Mg2+, and Mn2+, but inhibited by Cu2+, Fe2+, and Zn2+. Herinase exhibited maximum activity at 30 °C and pH 7.0. These results demonstrate that herinase could be a novel fibrinolytic enzyme. 相似文献
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