Summary
The effects of various denaturing conditions on the activity of purified rabbit muscle amylo-1,6-glucosidase/oligo-1,4 → 1,4-glucantransferase were investigated. The two enzymatic activities were measured independently of each other as well as by their combined action on glycogen phosphorylase limit dextrin. Arrhenius plots, activity measurements in the presence of urea, and activity measurements following preincubation in urea suggest that the single polypeptide protein may undergo conformational changes under these various conditions which could alter the behavior of the two activities.
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This work was supported in part by grants from the U.S. Public Health Service, National Institutes of Health (AM-13950) and The Robert A. Welch Foundation (Q-402).
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Nelson, T.E., Watts, T.E. The effect of denaturing conditions on the activity of rabbit muscle amylo-1,6-glucosidase/oligo-1,4 → 1,4-glucantransferase. Mol Cell Biochem 5, 153–159 (1974). https://doi.org/10.1007/BF01731378
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DOI: https://doi.org/10.1007/BF01731378