PROPERTIES OF ACID BETA-D-GALACTOSIDASE ISOLATED FROM I-CELL DISEASE BRAIN AND SPLEEN

被引：5

作者：

MILLER, AL ^{[1
]}

LEVITT, P ^{[1
]}

INGRAHAM, H ^{[1
]}

CONVERSE, J ^{[1
]}

LEWIS, L ^{[1
]}

机构：

[1] UNIV CALIF SAN DIEGO,DEPT NEUROSCI,LA JOLLA,CA 92093

来源：

JOURNAL OF NEUROCHEMISTRY | 1979年 / 32卷 / 05期

关键词：

D O I：

10.1111/j.1471-4159.1979.tb11088.x

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：

Abstract— Acid 4‐methylumbelliferyl β‐d‐galactosidase activity from autopsied I‐cell disease brain and spleen tissues was 28% and 35% respectively of normal activity. Acid β‐d‐gatactosidase (β‐d‐galactoside galactohydrolase, EC 3.2.1.23) from two I‐cell disease brains demonstrated a 5‐fold increase over normal for the proportion of enzyme activity which did not adsorb to Concanavalin A‐Sepharose 4B, while acid β‐d‐galactosidase from two I‐cell disease spleens demonstrated a 21–35‐fold increase in the proportion of unadsorbed enzyme activity. Normal and I‐cell disease acid β‐d‐galactosidase present in crude brain and spleen supernatant fluids and in preparations partially purified on Concanavalin A‐Sepharose 4B had similar apparent Km values with respect to 4‐methylumbelliferyl β‐d‐galactopyranoside and GM1‐ganglioside. Isoelectric focusing profiles of normal and I‐cell disease acid β‐d‐galactosidase from crude brain and spleen‐supernatant fluids and partially purified preparations were similar. Neuraminidase treatment and subsequent isoelectric focusing of the partially purified normal and I‐cell disease enzyme preparations from brain and spleen revealed increases in the proportion of I‐cell β‐d‐galactosidases found at neutral pH values, suggesting that the electrophoretic variations observed for the I‐cell enzymes may not be attributed solely to changes in sialic acid composition. Copyright © 1979, Wiley Blackwell. All rights reserved

引用

页码：1479 / 1485

页数：7

共 45 条

[1] INHIBITION OF RAT CLEARANCE SYSTEM FOR AGALACTO-OROSOMUCOID BY YEAST MANNANS AND BY MANNOSE [J].