Spectroscopic studies on the denaturation of papain solubilized and Triton X-100-solubilized glucoamylase from rabbit small intestine
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Intestinal brush border proteins consist of an enzymatically active hydrophilic moiety attached to a hydrophobic tail. Papain dissociates the hydrophilic part by cleaving off the hydrophobic tail, whereas the detergentTriton X-100 solubilizes the whole molecule. Denaturation by 8 M urea or 4 M guanidinium chloride does not alter the structure of the papain-solubilized enzyme. An appreciable alteration of the structure of detergent-solubilized enzyme was observed on denaturation. The difference spectra of Triton X-100 (1%)—solubilized enzyme and its urea denatured form shifts and intensifies, with increase in the concentration of the denaturant with an isobestic point at 252 nm. A new band at 280 nm also appears at 4 M urea concentration. Papain-solubilized glucoamylase has an ∞ -helical conformation in solution unlike the detergentsolubilized fraction. An elongated structure for the papain solubilized enzyme is inferred from the urea denaturation studies and from molecular weight determinations.
KeywordsRabbit small intestine glucoamylase papain denaturation Triton X-100 difference spectra
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- Nirmala Murthy, T. (1978)Studies on Triton X-100 solubilized glucoamylase from rabbit small intestine, M. Phil Dissertation, University of Hyderabad, Hyderabad.Google Scholar