MOLECULAR-SIZE OF N-ACETYLGLUCOSAMINYLPHOSPHOTRANSFERASE AND ALPHA-N-ACETYLGLUCOSAMINYL PHOSPHODIESTERASE AS DETERMINED INSITU IN GOLGI MEMBRANES BY RADIATION INACTIVATION

被引：8

作者：

BENYOSEPH, Y

POTIER, M

PACK, BA

MITCHELL, DA

MELANCON, SB

NADLER, HL

机构：

[1] WAYNE STATE UNIV, CS MOTT CTR HUMAN GROWTH & DEV, SCH MED, DEPT PEDIAT, DETROIT, MI 48201 USA

[2] WAYNE STATE UNIV, CS MOTT CTR HUMAN GROWTH & DEV, SCH MED, DEPT BIOCHEM, DETROIT, MI 48201 USA

[3] WAYNE STATE UNIV, CS MOTT CTR HUMAN GROWTH & DEV, SCH MED, DEPT OBSTET & GYNECOL, DETROIT, MI 48201 USA

[4] UNIV MONTREAL, HOP ST JUSTINE, GENET MED SECT, MONTREAL H3T 1C5, QUEBEC, CANADA

来源：

BIOCHEMICAL JOURNAL | 1986年 / 235卷 / 03期

关键词：

D O I：

10.1042/bj2350883

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 radiation inactivation method was used to determine the molecular size of the two enzymes that participate in the synthesis of the phosphomannosyl recognition marker of lysosomal proteins. The determinations were carried out in situ, in Golgi membranes isolated from normal human placenta and cultured skin fibroblasts. A molecular size of 228 .+-. 29 kDa was found for placental N-acetylglucosaminyl-phosphotransferase, and 129 .+-. 11 kDa for placental .alpha.-N-acetylglucosaminyl phosphodiesterase. The values for the fibroblast enzymes were about 20% higher, 283 .+-. 27 kDa and 156 .+-. 14 kDa for the transferase and phosphodiesterase respectively. Triton X-100 had no effect on the molecular size of these enzymes.

引用

页码：883 / 886

页数：4

共 20 条

[1] RADIATION INACTIVATION OF MEMBRANE-PROTEINS - MOLECULAR-WEIGHT ESTIMATES INSITU AND AFTER TRITON-X-100 SOLUBILIZATION [J].