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The Nature of Resistance of the Coagulation Factor XIII Structure to Hypochlorite-Induced Oxidation
Doklady Biochemistry and Biophysics ( IF 0.8 ) Pub Date : 2020-12-25 , DOI: 10.1134/s1607672920050117
A D Vasilyeva 1 , L V Yurina 1 , A E Bugrova 1 , M I Indeykina 1, 2 , A S Kononikhin 3 , A N Schegolikhin 1 , V S Ivanov 1 , E N Nikolaev 4 , M A Rosenfeld 1
Affiliation  

Abstract

The damage to blood coagulation factor XIII (FXIII) at different stages of its enzymatic activation under the action of various physiological amounts of hypochlorite ion was studied. The results obtained by HPLC-MS/MS, SDS-PAGE, and colorimetry showed that, during the conversion of FXIII to FXIIIa, the vulnerability of FXIII to hypochlorite-induced oxidation increased. FXIII oxidized with 150 μM hypochlorite completely retained its enzymatic activity inherent to the intact protein, whereas FXIIIa treated with 50 μM hypochlorite showed sharply reduced enzymatic activity. It was shown that a number of methionine and cysteine residues on the catalytic subunit can perform antioxidant function; additionally, the regulatory subunits of FXIII-B contribute to the antioxidant protection of the catalytic center of the FXIII-A subunit, which, together with the tight packing of the tetrameric structure of the FXIII proenzyme, are the three factors that provide high protein resistance to the oxidizing agent.



中文翻译:

凝血因子XIII结构对次氯酸盐诱导的氧化的抗性性质

摘要

研究了在各种生理量的次氯酸根离子的作用下,凝血因子XIII(FXIII)在其酶促活化的不同阶段的损伤。通过HPLC-MS / MS,SDS-PAGE和比色法获得的结果表明,在FXIII转化为FXIIIa的过程中,FXIII对次氯酸盐诱导的氧化的脆弱性增加。用150μM次氯酸盐氧化的FXIII完全保留了完整蛋白固有的酶促活性,而用50μM次氯酸盐处理的FXIIIa则显着降低了酶促活性。结果表明,催化亚基上的许多蛋氨酸和半胱氨酸残基具有抗氧化功能。此外,FXIII-B的调节性亚基有助于FXIII-A的催化中心的抗氧化保护,

更新日期:2020-12-25
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