Degradation of the human erythrocyte membrane band 3 studied with the monoclonal antibody directed against an epitope on the cytoplasmic fragment of band 3
European Journal of Biochemistry, ISSN: 1432-1033, Vol: 174, Issue: 4, Page: 647-654
1988
- 36Citations
- 7Captures
- 3Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations36
- Citation Indexes35
- 35
- CrossRef32
- Policy Citations1
- Policy Citation1
- Captures7
- Readers7
- Mentions3
- References3
- Wikipedia3
Article Description
The mouse hybridoma monoclonal antibody BIII.136 of the IgG2a class is specific for human erythrocyte band‐3 protein. It was shown by means of immunoblotting and immunoprecipitation assays that the antibody recognized an epitope located in the cytoplasmic pole of the band‐3 molecule within approximately 20 kDa from the N‐terminal end. The N‐terminal fragments of band‐3 protein, migrating in SDS/polyacrylamide gel electrophoresis in the 60‐kDa, 40‐kDa and 20‐kDa regions, were detected with the antibody in untreated red‐cell membranes as products of autolysis of band‐3 protein. A correlation was found between the amount of these fragments and erythrocyte age, which suggests that partial degradation of band 3 proceeds in vivo during senescence of erythrocytes. The further degradation of band‐3 protein in vitro was not observed in intact erythrocytes stored at 4°C, but progressed distinctly after hemolysis of red cells, during washing and storing the membranes. Copyright © 1988, Wiley Blackwell. All rights reserved
Bibliographic Details
Wiley
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