Literature DB >> 29613

The relation of the pH and concentration-dependent dissociation of porcine heart mitochondrial malate dehydrogenase.

D C Wood, C T Hodges, J H Harrison.   

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Year:  1978        PMID: 29613     DOI: 10.1016/0006-291x(78)90874-4

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


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  3 in total

1.  Aggregation states of mitochondrial malate dehydrogenase.

Authors:  S A Sánchez; T L Hazlett; J E Brunet; D M Jameson
Journal:  Protein Sci       Date:  1998-10       Impact factor: 6.725

2.  Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5.

Authors:  J Chen; D L Smith
Journal:  Protein Sci       Date:  2001-05       Impact factor: 6.725

3.  Hydrophobic interaction between the monomer of mitochondrial malate dehydrogenase and phospholipid membranes.

Authors:  K A Webster; K B Freeman; S Ohki
Journal:  Biochem J       Date:  1980-01-15       Impact factor: 3.857

  3 in total

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