Abstract
It has been found that 7 out of 18 tested single amino-acid mutants of human haemoglobin can be distinguished from A 1 and the remainder are indistinguishable from A 1 by quantitative complement fixation tests with rabbit anti-A 1 sera. The mutations antigenically distinguishable from A 1 occur in regions of the haemoglobin molecule where the primary sequence of rabbit and human haemoglobin are found to vary. Mutations antigenically indistinguishable from normal A 1 are all located in regions of the primary sequence where rabbit and human haemoglobins are identical. The significance of this as regards the number of antigenic regions, the relationship of molecular structure to tolerance, and the molecular localization of possible antigenic determinants in human haemoglobin are discussed.
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