Literature DB >> 7263714

Localization of glyceraldehyde-3-phosphate dehydrogenase in intact human erythrocytes. Evaluation of membrane adherence is autoradiographs at low grain density.

M Solti, F Bartha, N Halász, G Tóth, F Sirokmán, P Friedrich.   

Abstract

Human erythrocytes were treated with highly tritiated [3H]iodoacetate under conditions when half of the label became attached to glyceraldehyde-3-phosphate dehydrogenase. After fixation, the cells were subjected to electron microscopic autoradiography. For the evaluation of distribution of grains, which were relatively few, a computerized method was developed. Statistical analysis of data showed the significant adherence of grains to the cell membrane. The results support the view that glyceraldehyde-3-phosphate dehydrogenase is localized near the membrane in the intact erythrocyte.

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Year:  1981        PMID: 7263714

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  3 in total

1.  Biochemical, immunological, and immunocytochemical evidence for the association of chalcone synthase with endoplasmic reticulum membranes.

Authors:  G Hrazdina; A M Zobel; H C Hoch
Journal:  Proc Natl Acad Sci U S A       Date:  1987-12       Impact factor: 11.205

2.  Glyceraldehyde-3-phosphate dehydrogenase release from erythrocytes during haemolysis. No evidence for substantial binding of the enzyme to the membrane in the intact cell.

Authors:  G T Rich; A P Dawson; J S Pryor
Journal:  Biochem J       Date:  1984-07-01       Impact factor: 3.857

3.  Oxidation of articular cartilage glyceraldehyde-3-phosphate dehydrogenase (G3PDH) occurs in vivo during carrageenin-induced arthritis.

Authors:  M S Baker; S Bolis; D A Lowther
Journal:  Agents Actions       Date:  1991-03
  3 in total

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