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PMID: 2822696 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Isolation of a cDNA encoding the muscle-specific subunit of human phosphoglycerate mutase.

The Journal of biological chemistry ·Vol. 262 ·No. 30 ·1987-10-25 ·Pages 14612-7

Shanske S, Sakoda S, Hermodson MA, DiMauro S, Schon EA

Abstract

We have isolated a full-length cDNA specifying the muscle-specific subunit of human phosphoglycerate mutase (PGAM-M). The cDNA encodes a deduced protein 253 amino acids in length and contains an unusually short (37 nucleotides) 3'-untranslated region. The deduced human PGAM-M protein is clearly related to yeast PGAM and to human diphosphoglycerate mutase. Genomic Southern analysis using the PGAM-M cDNA as a probe implies the presence of a large PGAM gene family in the human genome, while Northern analysis demonstrates tissue-specific transcription of this isoenzyme gene.

MeSH Terms
Amino Acid Sequence Base Sequence DNA/analysis,isolation & purification Humans Molecular Sequence Data Muscles/enzymology Nucleic Acid Hybridization Phosphoglycerate Mutase/analysis,genetics Phosphotransferases/genetics Protein Conformation
Chemicals
DNA Phosphotransferases Phosphoglycerate Mutase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Shanske S
H. Houston Merritt Clinical Research Center for Muscular Dystrophy and Related Disorders, Columbia University, College of Physicians & Surgeons, New York, New York 10032.
Sakoda S
Hermodson M A
DiMauro S
Schon E A
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1987-10-25
Pages
14612-7
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM15253 · United States
NINDS NIH HHS · NS11766 · United States
Databases
GENBANK
M18172
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