Localization of the amino acid substitution site in a new variant of human serum albumin, albumin Mexico-2

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Abstract
An electrophoretic screening procedure revealed 2 spp. of human serum albumin Mexico occur that are indistinguishable by conventional electrophoretic methods. These species may be referred to as albumins Mexico-1 and Mexico-2. Isolation and determination of the partial sequence of the cyanogen bromide fragment of albumin Mexico-2 that differs from the corresponding fragment of the common albumin A revealed this variant to arise from at least a glycine/aspartic acid substitution at position 550. This region of the albumin molecule is involved in the binding of the fatty acid, palmitate.