Literature DB >> 4212432

The membrane association and dissociation of human glyceraldehyde-3-phosphate dehydrogenase under various conditions of hemolysis. Immunochemical evidence for the lack of binding under cellular conditions.

D Maretzki, J Groth, A G Tsamaloukas, M Gründel, S Krüger, S Rapoport.   

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Year:  1974        PMID： 4212432     DOI： 10.1016/0014-5793(74)80022-0

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


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  5 in total

1.  Modification of glyceraldehyde 3-phosphate dehydrogenase activity by adsorption on phospholipid vesicles.

Authors:  M S Wooster; J M Wrigglesworth
Journal:  Biochem J       Date:  1976-12-01       Impact factor: 3.857

2.  Partial reversible inactivation of enzymes due to binding to the human erythrocyte membrane.

Authors:  M Solti; P Friedrich
Journal:  Mol Cell Biochem       Date:  1976-02-25       Impact factor: 3.396

3.  Interaction of NAD-dependent dehydrogenases with human erythrocyte membranes. Evidence that D-glyceraldehyde-3-phosphate dehydrogenase and lactate dehydrogenase are catalytically active in a membrane-bound state.

Authors:  V I Muronetz; N A Shcherbatova; N K Nagradova
Journal:  Appl Biochem Biotechnol       Date:  1996 Oct-Nov       Impact factor: 2.926

4.  Regulation of the interaction of purified human erythrocyte AMP deaminase and the human erythrocyte membrane.

Authors:  G M Pipoly; G R Nathans; D Chang; T F Deuel
Journal:  J Clin Invest       Date:  1979-05       Impact factor: 14.808

5.  A 1H n.m.r. study of the kinetic properties expressed by glyceraldehyde phosphate dehydrogenase in the intact human erythrocyte.

Authors:  K M Brindle; I D Campbell; R J Simpson
Journal:  Biochem J       Date:  1982-12-15       Impact factor: 3.857
  5 in total

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