PURIFICATION OF RAT-LIVER ARYLSUFATASE-A AND ITS MICROHETEROGENEITY ASSAYED BY CROSSED AFFINITY-IMMUNOELECTROPHORESIS

被引：0

作者：

WOJCZYK, B ^{[1
]}

HOJA, D ^{[1
]}

LITYNSKA, A ^{[1
]}

机构：

[1] JAGIELLONIAN UNIV,INST ZOOL,DEPT ANIM PHYSIOL,BIOSTRUCT RES LAB,INGARDENA 6,PL-30060 KRAKOW,POLAND

来源：

ACTA BIOCHIMICA POLONICA | 1992年 / 39卷 / 04期

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Arylsulfatase A (arylsulfatase sulfohydrolase) EC 3.1-6.1 was purified from rat liver by a procedure consisting of differential centrifugation, Con A-Sepharose and Blue Sepharose chromatography, PBE 94 chromatofocusing, DEAE-cellulose and gel filtration chromatography followed by preparative electrophoresis. A molecular mass of 132000 was estimated by gradient PAGE. Particular proteins were detected by immunoelectrophoresis. Isoelectric focusing combined with immunoelectrophoresis gave two peaks of arylsulfatase A, with isoelectric points of pH 3.9 and 4.5. Microheterogeneity of rat liver arylsulfatase A was studied by affinity immunoelectrophoresis with 9 different lectins. The presence of concanavalin A-, Lens culinaris agglutinin-, Lotus tetragonolobus agglutinin- and wheat germ agglutinin-reactive forms permitted assessment of the types of carbohydrate moieties in arylsulfatase A.

引用

页码：355 / 367

页数：13

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