The binding of nicotinamide-adenine dinucleotide to yeast d-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 56 ·No. 6 ·1966-12-00 ·Pages 1661-7

Kirschner K, Eigen M, Bittman R, Voigt B

Abstract

暂无摘要

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Kirschner K

MAX-PLANCK-INSTITUT FUR PHYSIKALISCHE CHEMIE, GOTTINGEN, GERMANY.

Eigen M

Bittman R

Voigt B

References (7)

7 references, click to expand

Comparison of experimental binding data and theoretical models in proteins containing subunits.
Biochemistry. 1966 Jan;5(1):365-85 PMID: 5938952
Yeast Glyceraldehyde-3-phosphate dehydrogenase. I. Electrophoresis of fractions precipitated by nucleic acid.
J Biol Chem. 1953 Feb;200(2):471-8 PMID: 13034804
The binding of diphosphopyridine nucleotide by yeast glyceraldehyde-3-phosphate dehydrogenase.
J Biol Chem. 1959 May;234(5):1286-92 PMID: 13654363
Feedback control by endproduct inhibition.
Cold Spring Harb Symp Quant Biol. 1961;26:301-12 PMID: 13923752
STRUCTURE OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE. STRUCTURE SYMMETRY WITHIN THE MOLECULE.
Nature. 1964 Dec 5;204:918-20 PMID: 14252370
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.
J Mol Biol. 1965 May;12:88-118 PMID: 14343300
Distinct subunits for the regulation and catalytic activity of aspartate transcarbamylase.
Biochemistry. 1965 Jun;4(6):1054-62 PMID: 5320387

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

Published

1966-12-00

Pages

1661-7

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC220150

External Links

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