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REVIEW OF LITERATURE 1 THE NONPRIMARY STRUCTURE OF HAEMOGLOBIN 2 THE DISSOCIATION OF HAEMOGLOBIN
CHEMISTRY OF THE DIFFERENT SUBUNITS
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a-chains acetic acid Acetone adult and foetal Amberlite IRC-50 amino acid amino acid substitutions animals anodic mobility arginine avian blood bovine breeds buffer buffer solution carboxymethylcellulose chain types chicken haemoglobin chromatographic behaviour chromatographic separation column compared corresponding demonstrated denaturation described Diagram dissociation distinguishable peptides dried electrophoresis electrophoresis at pH electrophoretic behaviour elution expl fingerprints fingerprints of adult foetal and adult foetal bovine foetal haemoglobin gene duplication globin glutathione haemoglobin components haemoglobin fractions haemoglobin Hb-Fj haemoglobin molecule haemoglobin types Hb-Ai Hb-Ai and Hb-Fi heterogeneity histidine Huisman human a-chains human haemoglobins hybridisation hydrochloric acid hydrolysis identical Ingram investigated isolated Jonxis lysine main component mammalian haemoglobins method mobility at pH molecular weight ninhydrin non-a-chains observed obtained ovine haemoglobins peptide pattern analysis percent polypeptide chains present procedure protein rabbit haemoglobin refer figure 11 room temperature ruminant single solution species spots Starch-gel electrophoresis structural differences subunits synthesized tryptic peptides tryptophane urea