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Glycogen phosphorylase is homodimeric (although the R state enzyme tends to be tetrameric in the absence of its glycogen substrate) consisting of two domains (N-terminal and C-terminal domains) made up of a core of pleated β-sheets flanked by α-helices. When alanine or cys- teine is used, most mutants will have significant activity, possibly equivalent to that of the wild-type transporter. (1985) Glutathione peroxidase activity in Parkinsons disease brain. , Chemical carcinogenesis, in Casarett and Doulls Toxicology The Basic Science of Poisons, 6th ed.
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