人胎盘酸性a-1,4葡萄糖苷酶的纯化研究  

The Pcurification of Human Placenta acid α-glucosidase

作　　者：唐玉珠[1] 尤颖健[2] 何善述[2] 

机构地区：[1]同济医科大学附属协和医院儿科,武汉430022 [2]同济医科大学生物化学教研室,武汉430030

出　　处：《华中科技大学学报（医学版）》1994年第S2期122-124,共3页Acta Medicinae Universitatis Scientiae et Technologiae Huazhong

摘　　要：本文对GAA的纯化进行了改良，通过CM-SephadexC-50离子交换、酸化沉淀、（NH_4)_2SO_4分段盐析和SephadexG-100亲和层析等步骤，从人胎盘中提纯了GAA，其比活性为698，729nmol（mgPto．h）^（-1），纯化倍数达3319.4倍，获得率为10．58％。IEF证明已达电泳单点纯，PI=4.7。PAGE上呈现两条蛋白带，与酶染位点一致，分子量分别为110kD和76kD。3319.4-fold purified acid α-glucosidase (GAA)was obtained from human placenta homogenation by CM-Sephadex C-50 ion-exchange,acidation, affinity chromatography.The specific activity of the purified GAA is 698729 nMol／mg·Pro· h and the yield is 10．58％．On IEF（PH range 3～9．5 or 3．5～5．5）electrophoresis，the purified GAA showed only one fluorescence band by enzymatic stain,and one protein band was at the same point after coomassie blue stain,with PI=4.7.3～28％ gradient PAGE of GAA revealed two enzyme components with molecular weights 110 kD and 76 kD,respectively.It was believed that the two components were GAA precursor and mature enzyme.

关 键 词：α-葡萄糖苷酶类 胎盘 分离和提纯 

分 类 号：R596[医药卫生—内科学]