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A comprehensive method to explore inhibitory kinetics and mechanisms of an anticoagulant peptide derived from Crassostrea gigas

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Food Science and Human Wellness 2022年第6期11卷 1491-1499页

作者： Shuzhen Cheng Di Wu Hanxiong Liu Xianbing Xu Beiwei Zhu Ming Du Department of Food Science and Engineering National Engineering Research Center of SeafoodDalian Polytechnic UniversityDalian 116034China Beijing Advanced Innovation Center for Food Nutrition and Human Health College of Food Science and Nutritional EngineeringChina Agricultural UniversityBeijing 100083China

A comprehensive method was applied to evaluate the anticoagulant activity of a novel anticoagulant peptide(NAESLRK)derived from oyster(Crassostrea gigas).The anticoagulant peptide drastically reduced the extrinsic clotting activity and also impaired the intrinsic clotting activity *** with clotting data,the thrombin peak height was reduced to 84.7 nmol/L from 123.4 nmol/L,and thrombin generation time was delayed to 4.67 min from 4.42 min when the extrinsic trigger was *** inhibitory kinetics of FⅪa,FⅨa,FⅩa,FⅡa,and APC in a purified component system rationally explained the reduction of extrinsic clotting activity and impairment of thrombin *** the inhibition of FⅩa and FⅡa activity,the activation processes of FⅩand FⅡby intrinsic/extrinsic tenase complex and prothrombinase were also *** anticoagulant activity in the plasma system was the result of comprehensive inhibition of various *** research provided a novel method for anticoagulant evaluation and inhibitory mechanism of bioactive peptides from food products.

关键词： Oyster Anticoagulant peptide inhibitory kinetics Coagulation factor Non-specific inhibitor

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Effect of Cationic Surfactant on the Inhibition of Ligninase by Hydrogen Peroxide

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Chinese Chemical Letters 2003年第8期14卷 836-839页

作者： ZhuanNiYU XiRong,HUANG ShaoFangSONG DanWANG XueMeiLU YueZhongLI YinBoQU PeiJiGAO KeyLabforColloidandInterfaceChemistryoftheEducationMinistryofChina ShandongUniversityJinan250100 KeyLabforColloidandInterfaceChemistryoftheEducationMinistryofChina ShandongUniversityJinan250100 StateKeyLabofMicrobialTechnologyOfChina ShandongUniversityJinan250100 StateKeyLabofMicrobialTechnologyOfChina ShandongUniversityJinan250100

The inhibition of ligninase by hydrogen peroxide in the presence of cationic surfactant CTAB was studied by kinetic spectrophotometric technique. Results showed that addition of CTAB enhanced the inhibition by H2O2, but it did not alter the inhibition pattern and the inhibition constant changed little with the concentration of CTAB. Modification of the enzymic protein by the surfactant monomer may be responsible for the above mentioned results.

关键词： Ligninase hydrogen peroxide cationic surfactant inhibitory kinetics veratryl alcohol.

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