Abstract
1. 1. Two α- and three β-subunits are assigned to the individual haemoglobin components of the rat Rattus norvegiens, detected after electrophoresis in polyacrylamide. 2. 2. Evidence is presented that the starch gel electrophoretic pattern is rendered complex by double-band formation of the individual haemoglobin components, due to partial ionization of an α-subunit cysteine residue, observed by Chua and Carrell (1974). 3. 3. Following alkylation by iodoacetamide, rat haemoglobins resolved in starch gel and in polyacrylamide gel into the same electrophoretic pattern. The identity of the two patterns was also achieved by an addition of ammonium persulphate to the starch gel.
Published Version
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