PMID: 4311Mar 16, 1976

Algal glyceraldehyde-3-phosphate dehydrogenase. Pyridine-nucleotide requirements of two enzymes purified from Scenedesmus obliquus

European Journal of Biochemistry
M J O'Brien, R Powls

Abstract

Two enzymes with glyceraldehyde-3-phosphate dehydrogenase activity have been purified from heterotrophically grown Scenedesmus obliquus by ion-exchange chromatography and gel filtration. The D-enzyme has a molecular weight of 550000 and a VNADH: VNADPH ratio of 16 whereas the T-enzyme has a molecular weight of 140000 and a VNADH:VNADPH ratio of 0.15. The two enzymes, however, are very similar with regard to their Michaelis constants for the reduced pyridine nucleotides, pH optimum, subunit size and ultraviolet absorption.

References

Oct 10, 1968·Biochemical and Biophysical Research Communications·B A MelandriP Pupillo
Apr 4, 1969·Analytical Biochemistry·J Babul, E Stellwagen
Dec 28, 1964·Annals of the New York Academy of Sciences·B J DAVIS
Nov 1, 1965·Plant Physiology·G A Hudock, R C Fuller
Aug 1, 1973·Plant Physiology·G J Kelly, M Gibbs

Citations

Mar 24, 2000·Plant Science : an International Journal of Experimental Plant Biology· Gómez Casati DFA A Iglesias

Related Concepts

Chlorophyta
Glyceraldehyde-3-Phosphate Dehydrogenases
Hydrogen-Ion Concentration
Alloenzymes
NADH
NADP
Spectrophotometry, Ultraviolet

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