The beta 2 subunit of human placenta hexosaminidase (Hex) A and B is a non-random association of the two polypeptides beta a and beta b.
The subunit structures of placental Hex A and B have previously been assigned as alpha beta 2 and 2 beta 2, respectively. The beta 2 subunit is composed of two non-identical polypeptide chains, beta a and beta b. Purified Hex A and B were fractionated on a chromatofocusing column, and the fractions were reduced and then alkylated with iodo-1-14C-acetamide. The polypeptide chains were separated by polyacrylamide-gel isoelectric focusing. From the radioactivity measurements of the polypeptides a constant value for beta a/beta b was obtained in all the chromatofocusing fractions, demonstrating a non-random structure of (beta a beta b) in each beta 2 subunit.
D005260:Female; D054818:Hexosaminidase A; D006596:Hexosaminidases / Q000302:isolation & purification*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D046911:Macromolecular Substances; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D001619:beta-N-Acetylhexosaminidases
D046911:Macromolecular Substances; D006596:Hexosaminidases; D054818:Hexosaminidase A; D001619:beta-N-Acetylhexosaminidases