Literature DB >> 4311

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

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.

Entities:  

Mesh:

Substances:

Year:  1976        PMID: 4311     DOI: 10.1111/j.1432-1033.1976.tb10218.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  2 in total

1.  Expression and characterization of pea chloroplastic glyceraldehyde-3-phosphate dehydrogenase composed of only the B-subunit.

Authors:  A D Li; L E Anderson
Journal:  Plant Physiol       Date:  1997-11       Impact factor: 8.340

2.  Characterization of two glyceraldehyde-3-phosphate dehydrogenase isoenzymes from the pentalenolactone producer Streptomyces arenae.

Authors:  K H Maurer; F Pfeiffer; H Zehender; D Mecke
Journal:  J Bacteriol       Date:  1983-02       Impact factor: 3.490

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.