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- W2023168219 abstract "Abstract A method is described for the purification of thyroid acid proteinase from extracts of pig thyroid glands. Weight-average molecular weight determinations are used to show that the enzyme undergoes a pH- and temperature-dependent dimerization reaction in 0.10 ionic strength buffers, involving monomers of molecular weight 21 000. The extent of dimerization is maximal at the isoelectric point of the enzyme (pH 7.5) and decreases as the net charge borne by the protein increases. Also, at pH 7.5 an increase of temperature from 1–25° favours dimer formation. The amino acid composition of the proteinase is reported, and it is shown that glycine is the only major component evident in N-terminal analysis. The enzyme is active against haemoglobin as substrate (37° and pH 3.6) and is inhibited to the extent of 90–100% by the pepsin inhibitor, diazoacetyl- dl -norleucine methyl ester. As with pepsin, only one dicarboxylic acid residue appears to be involved in reaction with the inhibitor. Studies with radioactively labelled thyroglobulin (alone and in thyroid extracts) as substrate indicate that the inhibitor is partially effective in preventing proteolysis by acid proteinase of its natural substrate." @default.
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- W2023168219 date "1969-02-01" @default.
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- W2023168219 title "Thyroid acid proteinase Properties and inactivation by diazoacetyl-norleucine methyl ester" @default.
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- W2023168219 doi "https://doi.org/10.1016/0005-2744(69)90162-4" @default.
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