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Abnormal human hemoglobins X. A study of hemoglobin leporeBoston
Affiliation:1. Prenatal Diagnostic Center, Guangxi Zhuang Autonomous Region Women and Children Care Hospital, Nanning, Guangxi, PR China;2. Prenatal Diagnostic Center, Yulin Women and Children Health Care Hospital, Yulin, Guangxi, PR China;1. Department of Biological Sciences and Health, Federal University of Amapá, Macapá, Brazil;2. Maternal, Infant and Psychiatric Nursing Department, University of São Paulo, School of Nursing, São Paulo 41633, Brazil;1. Centre for Research and Development of Medical Diagnostic Laboratories, Faculty of Associated Medical Sciences Khon Kaen University, Khon Kaen, Thailand;2. Medical Science Program, Graduate School, Khon Kaen University, Thailand
Abstract:An abnormal hemoglobin has been isolated from two related individuals of Italian extraction. This abnormal hemoglobin has been identified with hemoglobin LeporeBoston on the basis of the fingerprinting pattern. Chemical studies have been performed on the “core” of this hemoglobin Lepore. Tryptic digestion after carboxy-methylation has been found to be the most suitable procedure for analyzing the “core” of the non-α chains. The fingerprinting analysis of the carboxymethylated hemoglobin has given sufficient information on the structure of this hemoglobin to pinpoint accurately the region along the amino acid sequence of the abnormal peptide chains, where the δ-like portion of these chains is joined to the β-like portion. Evidence has been obtained to show that the abnormal peptide chains of hemoglobin Lepore are equal in length to either β- or δ-chains (146 amino acids).
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