THE ACTIVITY OF PARAFUSIN IS DISTINCT FROM THAT OF PHOSPHOGLUCOMUTASE IN THE UNICELLULAR EUKARYOTE PARAMECIUM

被引：17

作者：

ANDERSEN, AP

WYROBA, E

REICHMAN, M

ZHAO, H

SATIR, BH

机构：

[1] YESHIVA UNIV ALBERT EINSTEIN COLL MED,DEPT ANAT & STRUCT BIOL,BRONX,NY 10461

[2] M NENCKI INST EXPTL BIOL,PL-02093 WARSAW,POLAND

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 200卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.1600

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：

In this paper we identified the presence of a Paramecium phosphoglucomutase enzymatic activity which is clearly distinct from that of parafusin - the exocytosis-related phosphoglycoprotein. Since the recently cloned parafusin showed homology to rabbit muscle phosphoglucomutase, we have designed a specific peptide parafusin antibody - generated to a region not present in any known sequenced phosphoglucomutases - to distinguish parafusin from the Paramecium phosphoglucomutase. Separation of these two proteins was obtained using liquid chromatography, enzymatic activity assay and immunoblotting analysis with the specific parafusin peptide antibody. Parafusin fractions incorporated [beta(35)S]UDP-Glc but not [S-35]Glc-1-P, whereas Paramecium phosphoglucomutase fractions incorporated [S-35]Glc-1-P but not [beta(35)S]UDP-Glc. This indicates that these two proteins are separate entities exhibiting different properties and most likely distinct functions in the cell. (C) 1994 Academic Press, Inc.

引用

页码：1353 / 1358

页数：6

共 21 条

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