Why the linkage of glycogen to glycogenin was so difficult to determine

William J. Whelan

doi:10.1002/bmb.96

Why the linkage of glycogen to glycogenin was so difficult to determine

William J. Whelan

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

3 Scopus citations

Abstract

Glycogenin is the self-glucosylating enzyme that primes mammalian and yeast glycogen synthesis. It proved to be the long-suspected, covalently bound protein component of glycogen. One of the most difficult aspects in elucidating the role of glycogenin was to learn the nature of its covalent bond to glycogen.

Original language	English (US)
Pages (from-to)	313-315
Number of pages	3
Journal	Biochemistry and Molecular Biology Education
Volume	35
Issue number	5
DOIs	https://doi.org/10.1002/bmb.96
State	Published - Sep 2007

Keywords

Glycogen
Glycogenin

ASJC Scopus subject areas

Biochemistry
Molecular Biology

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10.1002/bmb.96

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abstract = "Glycogenin is the self-glucosylating enzyme that primes mammalian and yeast glycogen synthesis. It proved to be the long-suspected, covalently bound protein component of glycogen. One of the most difficult aspects in elucidating the role of glycogenin was to learn the nature of its covalent bond to glycogen.",

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Why the linkage of glycogen to glycogenin was so difficult to determine

Abstract

Keywords

ASJC Scopus subject areas

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