Literature DB >> 5844084

Alternative forms of triosephosphate dehydrogenase in Chromatium.

G A Hudock, D B Mellin, R C Fuller.   

Abstract

Triosephosphate dehydrogenase was purified extensively from the obligately phototrophic bacterium Chromatium. Enzyme prepared from photolithotrophically grown cells differed in several properties from enzyme prepared from photoorganotrophically grown cells. Either form of the enzyme could be transformed in vitro to the other by mild oxidation or reduction, which effected both Michaelis constants and reactive -SH contents of the proteins.

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Year:  1965        PMID: 5844084     DOI: 10.1126/science.150.3697.776

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  1 in total

1.  Tissue-characteristic forms of glyceraldehyde 3-phosphate dehydrogenase.

Authors:  N Ressler; S Lee
Journal:  Biochem J       Date:  1970-08       Impact factor: 3.857

  1 in total

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