• Spectroscopic studies on the denaturation of papain solubilized and Triton X-100-solubilized glucoamylase from rabbit small intestine

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    • Keywords


      Rabbit small intestine; glucoamylase; papain denaturation; Triton X-100; difference spectra

    • Abstract


      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.

    • Author Affiliations


      S Sivakami1 D Chatterji1

      1. School of Life Sciences, University of Hyderabad, Hyderabad - 500 134
    • Dates

  • Journal of Biosciences | News

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      Posted on July 25, 2019

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