N-terminal amino acid analysis reveal peptide heterogeneity in major electrophoretic protein components of erythrocyte ghosts
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference13 articles.
1. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
2. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes
3. Study of the Dansylation Reaction of Amino Acids, Peptides and Proteins
Cited by 46 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Kell blood group antigens are part of a 93,000-dalton red cell membrane protein.;Journal of Biological Chemistry;1986-07
2. Spectrin Domains: Proteolytic Susceptibility as a Probe of Protein Structure;Journal of Cellular Biochemistry;1982
3. Structural characterization of the phosphorylation sites of human erythrocyte spectrin.;Journal of Biological Chemistry;1980-12
4. Identification of proteolytically resistant domains of human erythrocyte spectrin.;Proceedings of the National Academy of Sciences;1980-10-01
5. Spectrin: Present status of a putative cyto-skeletal protein of the red cell membrane;The Journal of Membrane Biology;1979-06
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