The 60 and 63 kDa proteolytic peptides of the red cell membrane band-3 protein: their prevalence in human and non-human primates
✍ Scribed by Marcos Palatnik; Maria Lucia Marti Silva Simões; Zoraide Maia Salomão Alves; Nanci Souto Maior Laranjeira
- Publisher
- Springer
- Year
- 1990
- Tongue
- English
- Weight
- 769 KB
- Volume
- 86
- Category
- Article
- ISSN
- 0340-6717
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✦ Synopsis
Three phenotypes based on the polymorphism of band-3 protein from human red cells are described. Limited proteolysis of intact red cells from most individuals (homozygotes) yields a peptide of 60 kDa, but in some cases (heterozygotes), there is also a 63-kDa peptide, and rarely only the single peptide of 63kDa is found. This is the first description of the 63-kDa homozygote. The interpretation that the three phenotypes are controlled by two alleles of a single autosomal locus, with no dominance, is supported by population and family studies. The frequencies of the allele, which we designate as p63, is 0.041 4-0.0068 in Caucasoids and 0.125 _+ 0.0121 in Negroids. The electrophoretic profiles and molecular weights of the peptides obtained with several commercial proteases from Streptornyces griseus are similar to those obtained with chymotrypsin. Whereas band-3 protein in two New-World monkeys (Saimiri and Cebus) resisted pronase attack, an Old-World monkey (Macaca mulatta) was monomorphic for a 63-kDa fragment, and in an ape (Pan troglodytes), a doublet of 62kDa and 64kDa was found. Band-3 protein polymorphism appears to be a good marker for genetic differentiation in human populations.
📜 SIMILAR VOLUMES
Several methods were tested for separating the major glycoproteins from other proteins extracted from human red cell membranes by the nondenaturing detergent, Triton X-100. Separation could be achieved by isoelectric focusing, but the intrinsic proteins (predominantly band 3) become irreversibly pre