The subunit structures of placental Hex A and B have previously been assigned as βa and βb, respectively. The β2 subunit is composed of two non-identical polypeptide chains, βa and βb. Purified Hex A and B were fractionated on a chromatofocusing column, and the fractions were reduced and then alkylated with iodo-I-14C-acetamide. The polypeptide chains were separated by polyacrylamide-gel isoelectric focusing. From the radioactivity measurements of the polypeptides a constant value for β2 was obtained in all the chromatofocusing fractions, demonstrating a non-random structure of (β2) in each β2 subunit.

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