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.
The β2 subunit of human placenta hexosaminidase (Hex) A and B is a non-random association of the two polypeptides αa and βb
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B. O'Dowd, D. Mahuran, J. A. Lowden; The β2 subunit of human placenta hexosaminidase (Hex) A and B is a non-random association of the two polypeptides αa and βb. Biosci Rep 1 January 1984; 4 (1): 59–63. doi: https://doi.org/10.1007/BF01120824
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