Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose-1-phosphate adenylyltransferase (EC 2.7.7.27)

Thomas H Haugen; Armana Ishaque; Jack Preiss

doi:10.1016/S0021-9258(19)57016-8

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Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose-1-phosphate adenylyltransferase (EC 2.7.7.27)

Journal article

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Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose-1-phosphate adenylyltransferase (EC 2.7.7.27)

Thomas H Haugen, Armana Ishaque and Jack Preiss

The Journal of biological chemistry, Vol.251(24), pp.7880-7885

12/25/1976

DOI: 10.1016/S0021-9258(19)57016-8

PMID: 826540

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Abstract

ADP-glucose pyrophosphorylase has been isolated in homogeneous form from an Escherichia coli B mutant, AC70R1, derepressed in the synthesis of glycogen synthetic enzymes. The enzyme has been found to be identical with the wild type enzyme with respect to kinetic properties, molecular weight, and immunological reactivity. The AC70R1 enzyme is composed of four identical subunits of molecular weight of approximately 50,000. This is based on the findings that: (a) gel electrophoresis under denaturing conditions shows only one component; (b) tryptic mapping shows only enough peptides to account for a single polypeptide subunit; (c) digestion with carboxypeptidase B releases stoichiometric amounts of arginine; and (d) NH2-terminal sequencing shows a single sequence for the first 27 residues.

Amino Acid Sequence

Molecular Weight

Nucleotidyltransferases - isolation & purification

Immunodiffusion

Amino Acids - analysis

Dithionitrobenzoic Acid

Adenosine Diphosphate Glucose

Carboxypeptidases

Macromolecular Substances

Escherichia coli - metabolism

Glycogen - biosynthesis

Protein Binding

Kinetics

Nucleotidyltransferases - metabolism

Details

Title: Subtitle: Biosynthesis of bacterial glycogen. Characterization of the subunit structure of Escherichia coli B glucose-1-phosphate adenylyltransferase (EC 2.7.7.27)
Creators: Thomas H Haugen
Armana Ishaque
Jack Preiss
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.251(24), pp.7880-7885
DOI: 10.1016/S0021-9258(19)57016-8
PMID: 826540
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Language: English
Date published: 12/25/1976
Academic Unit: Pathology
Record Identifier: 9984047856802771

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