Literature DB >> 5687820

Lactate dehydrogenase isozymes: dissociation and denaturation by dilution.

C L Markert, E J Massaro.   

Abstract

The tetrameric enzyme lactate dehydrogenase dissociates into its constituent monomeric subunits in a high ion to protein concentration ratio, in certain ionic environments when frozen, and at extreme dilution. Dissociation by dilution involves changes in tertiary conformation which inactivate the enzyme. The dissociation is strongly inhibited by homologous native proteins, but only slightly by denatured or unrelated proteins.

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Year:  1968        PMID: 5687820     DOI: 10.1126/science.162.3854.695

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


  5 in total

1.  Evidence for the lack of feedback regulation of gene activity and for the absence of subunit exchange between lactate dehydrogenase tetramers in vivo.

Authors:  B Nadal-Ginard
Journal:  Proc Natl Acad Sci U S A       Date:  1976-10       Impact factor: 11.205

2.  Calculation of the free energy of association for protein complexes.

Authors:  N Horton; M Lewis
Journal:  Protein Sci       Date:  1992-01       Impact factor: 6.725

3.  Some effects of polyvinyl alcohol and polyvinyl pyrrolidone on the activity of lactate dehydrogenase and its isoenzymes. Histochemical and biochemical studies.

Authors:  H A Dahl; S H From
Journal:  Histochemie       Date:  1971

4.  Selective inactivation of lactate dehydrogenase of rat tissues by sodium deoxycholate.

Authors:  T Lehnert; H H Berlet
Journal:  Biochem J       Date:  1979-03-01       Impact factor: 3.857

5.  Purificationa and properties of a fructose-1,6-diphosphate-activated lactate dehydrogenase from Streptococcus faecalis.

Authors:  C L Wittenberger; N Angelo
Journal:  J Bacteriol       Date:  1970-03       Impact factor: 3.490

  5 in total

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