Band 3 protein of the red cell membrane of the llama: crosslinking and cleavage of the cytoplasmic domain |
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| Authors: | J K Khodadad R S Weinstein |
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| Affiliation: | 1. Department of Pathology, Rush Medical College, Chicago, Illinois 60612 USA;2. Department of Anatomy, Rush Medical College, Chicago, Illinois 60612 USA;3. Rush-Presbyterian-St. Luke''s Medical Center, Chicago, Illinois 60612 USA;1. CRRC Zhuzhou Electric Locomotive Research Institute Co., Ltd., Huazhong University of Science and Technology, Wuhan 430074, China;2. School of Hydropower and Information Engineering, Huazhong University of Science and Technology, Wuhan 430074, China;1. College of Veterinary Medicine, Qingdao Agricultural University, Qingdao, 266109, China;2. Key Laboratory of Etiology and Epidemiology of Emerging Infectious Diseases in Universities of Shandong, Shandong First Medical University & Shandong Academy of Medical Sciences, Tai’an, 271000, China;1. The Comprehensive Cancer Center & Shanghai Key Laboratory for Pancreatic Diseases, Shanghai First People''s Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 201620, China;2. Experimental Research Center, Shanghai First People''s Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 201620, China;3. Shanghai-MOST Key Laboratory of Health and Disease Genomics, Chinese National Human Genome Center, Shanghai 201203, China;4. The Department of Dermatology, Duke University Medical Center, Durham, NC 27710, USA;1. Section of Neonatology, Department of Pediatrics, Baylor College of Medicine, Houston, Texas;2. Basic Sciences Perinatology Research Laboratories, Department of Obstetrics and Gynecology, Baylor College of Medicine, Houston, Texas;3. Department of Pathology and Genomic Medicine, Houston Methodist Hospital, Houston, Texas;1. Department of Informatics, University of Milano-Bicocca, Viale Sarca 336, 20126 Milano, Italy;2. Faculty of Design and ArtFree University of Bozen-Bolzano, Piazza Università 1, 39100 Bolzano, Italy;3. IRCCS Istituto Ortopedico Galeazzi, Via Galeazzi, 4, 20161 Milano, Italy |
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| Abstract: | Comparative studies were done on the cytoplasmic domain of the band 3 protein in the red cell membranes of the the human and the llama. Two approaches were used: crosslinking with o-phenanthroline/CuSO4, and cleavage with 2-nitro-5-thiocyanobenzoate. o-Phenanthroline/CuSO4 crosslinks the band 3 polypeptide chains in the human; in contrast band 3 in the llama is minimally crosslinked by this agent. 2-Nitro-5-thiocyanobenzoate cleaves band 3 in the human into a 23,000-dalton fragment; a similar fragment is not generated from the llama band 3. These studies show that the cysteine residue located 23,000 daltons from the N-terminus of band 3 in the human involved in these reactions is unavailable for crosslinking and cleavage in the llama. Species differences in the cytoplasmic domain of band 3 may contribute to the unusual resistance of llama red cells to osmotic, chemical and physically-induced deformation. |
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