STUDIES ON ASPIRIN ESTERASE OF HUMAN-SERUM
STUDIES ON ASPIRIN ESTERASE OF HUMAN-SERUM
复制标题
DOI：
10.1254/jjp.29.581
复制
发表时间：
1979-01-01
期刊：
影响因子：
--
通讯作者：
SUGIURA, M
中科院分区：
文献类型：
--
作者：
MORIKAWA, M;INOUE, M;SUGIURA, M
研究了人血清中的阿司匹林水解活性;发现阿司匹林水解活性在性别之间存在差异，并以从1 ml血清中释放的mU/ [mUnits]水杨酸表示。以mU水杨酸/ml白蛋白表示的阿司匹林水解活性没有显示出这种差异。在慢性肝炎、肝硬化和肾病患者中，阿司匹林水解活性远低于健康人。在圆盘电泳实验中，阿司匹林水解活性位于假胆碱酯酶和白蛋白中，胆碱酯酶区的活性被硫酸依地孕酮抑制。当从人血清中的白蛋白被纯化的色谱上的DEAE-纤维素和Sephadex G-100，纯化的白蛋白水解阿司匹林和这种阿司匹林水解活性的纯化的白蛋白，虽然不抑制硫酸乙二酯和氟磷酸二异丙酯，被抑制用乙酸酐处理。显然，人血清中阿司匹林水解活性包括对阿司匹林的乙酰化作用和假胆碱酯酶活性。
The aspirin-hydrolyzing activity in human serum was studied; a difference between the sexes in the aspirin-hydrolyzing activity was found and expressed in mU/ [mUnits] salicylic acid released from 1 ml of serum. Aspirin-hydrolyzing activity expressed in mU salicylic acid/ml albumin showed no such difference. In cases of chronic hepatitis, liver cirrhosis and nephrosis, the aspirin-hydrolyzing activity was much lower than seen in healthy persons. In disc electrophoretic experiments, the aspirin-hydrolyzing activity was located in pseudocholinesterase and albumin and the activity in the cholinesterase region was inhibited by eserine sulfate. When the albumin from human serum was purified by chromatography on DEAE-cellulose and Sephadex G-100, the purified albumin hydrolyzed aspirin and this aspirin-hydrolyzing activity of purified albumin, although not inhibited by eserine sulfate and diisopropyl fluorophosphate, was inhibited by treatment with acetic anhydride. Apparently the aspirin-hydrolyzing activity from human serum included the pseudocholinesterase activity and acetylation effect on aspirin.