Literature DB >> 4364620

Selective chemical modification of arginine residues in mitochondrial malate dehydrogenase.

M Foster, J H Harrison.   

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Year:  1974        PMID： 4364620     DOI： 10.1016/0006-291x(74)90921-8

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


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  7 in total

1.  Inhibition of the GTPase activity of transducin by an NAD+:arginine ADP-ribosyltransferase from turkey erythrocytes.

Authors:  P A Watkins; Y Kanaho; J Moss
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

2.  Functional arginyl residues as ATP binding sites of glutamine synthetase and carbamyl phosphate synthetase.

Authors:  S G Powers; J F Riordan
Journal:  Proc Natl Acad Sci U S A       Date:  1975-07       Impact factor: 11.205

3.  Chemical modification of enzymes: critical evaluation of the graphical correlation between residual enzyme activity and number of groups modified.

Authors:  E Stevens; R F Colman
Journal:  Bull Math Biol       Date:  1980       Impact factor: 1.758

4.  Essential arginine residues occur in or near the catalytic site of L-amino acid oxidase.

Authors:  M F Christman; J M Cardenas
Journal:  Experientia       Date:  1982-05-15

Review 5.  Arginyl residues and anion binding sites in proteins.

Authors:  J F Riordan
Journal:  Mol Cell Biochem       Date:  1979-07-31       Impact factor: 3.396

6.  Probing the function(s) of active-site arginine residue in Leishmania donovani adenosine kinase.

Authors:  M Ghosh; A K Datta
Journal:  Biochem J       Date:  1994-03-01       Impact factor: 3.857

7.  Dye-affinity labelling of bovine heart mitochondrial malate dehydrogenase and study of the NADH-binding site.

Authors:  N E Labrou; E Eliopoulos; Y D Clonis
Journal:  Biochem J       Date:  1996-04-15       Impact factor: 3.857
  7 in total

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