PURIFICATION AND PROPERTIES OF RABBIT MUSCLE AMYLO-1,6-GLUCOSIDASE-OLIGO-1,4-]1,4-TRANSFERASE

被引：65

作者：

NELSON, TE

KOLB, E

LARNER, J

机构：

[1] Department of Biochemistry, College of Medical Sciences, University of Minnesota, Minneapolis

[2] Department of Biochemistry, Mayo Graduate School of Medicine, Rochester, Minn.

来源：

BIOCHEMISTRY | 1969年 / 8卷 / 04期

关键词：

D O I：

10.1021/bi00832a017

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：

The glycogen phosphorylase limit dextrindebranchingsystem of muscle amylo-1,6-glucosidaseoligo-1,4→1,4-transferase was purified twofold overprevious preparations by a new procedure and itsproperties reinvestigated. The preparation was foundto be homogeneous by both physical and biologicalcriteria and apparently contains two distinct enzymatic activities.The pH optima in cationic buffers was found tobe at 6.6 whereas that in anionic buffers was shiftedto 7.2. Protonated hydroxylalkyl-substituted amineswere found to inhibit the glucosidase-transferase in asimple linear noncompetitive manner. A mechanism forthis type of inhibition is suggested. © 1969, American Chemical Society. All rights reserved.

引用

页码：1419 / &

共 46 条

[1] A NEW PATHWAY IN RABBIT MUSCLE FOR ENZYMATIC DEBRANCHING OF GLYCOGEN [J].