Literature DB >> 6642053

The identity of bovine liver "nothing dehydrogenase".

S I Hutchins, S M Williams, C R Geren.   

Abstract

An assay system was developed which allowed the partial purification of the substrate for beef liver nothing dehydrogenase. This was also found to be a substrate for lactate dehydrogenase (LDH). Using electrophoretic separations of purified LDH and beef liver extracts, nothing dehydrogenase was determined to be primarily the H4 isoenzyme of LDH. The nothing dehydrogenase phenomena was also observed with highly-purified, commercially-obtained LDH.

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Year:  1983        PMID: 6642053     DOI: 10.1016/0020-711x(83)90026-5

Source DB:  PubMed          Journal:  Int J Biochem        ISSN: 0020-711X


  3 in total

1.  In situ kinetic parameters of glucose-6-phosphate dehydrogenase and phosphogluconate dehydrogenase in different areas of the rat liver acinus.

Authors:  G N Jonges; C J Van Noorden
Journal:  Histochem J       Date:  1989 Sep-Oct

2.  On the nature of the 'nothing dehydrogenase' reaction.

Authors:  C J Van Noorden; A Kooij; I M Vogels; W M Frederiks
Journal:  Histochem J       Date:  1985-10

3.  In situ determination of different dehydrogenase activity profiles in the linings of odontogenic keratocysts and radicular cysts.

Authors:  G I Mason; J B Matthews
Journal:  Histochem J       Date:  1996-03
  3 in total

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