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. 1975 Dec;151(3):747–749. doi: 10.1042/bj1510747

The binding of nicotinamide-adenine dimucleotide to glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.

G Allen, J I Harris
PMCID: PMC1172424  PMID: 175789

Abstract

The binding of NAD+ to glyceraldehyde 3-phosphate dehydrogenase (EC 1.2.1.12) from Bacillus stearothermophilus has been studied by measurement of protein fluorescence quenching. Slight negative co-operativity was observed in the binding of the third and fourth coenzyme molecules to the tetrameric enzyme. The first two coenzyme molecules were tightly bound. In this respect the enzyme resembles that from sturgeon muscle rather than that from yeast.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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