The effect of guanidine hydrochloride on crystalline pepsin.
نویسندگان
چکیده
In a previous communication, it was shown that on prolonged exposure to urea at temperatures above 20” pepsin is irreversibly inactivated (1). The loss of activity is most marked in the pH range of 4.6 to 5.6 and is always accompanied by the formation of nonprotein material that originates from autodigestion of the protein. Since urea is known to affect the secondary structure of proteins by rupturing hydrogen bonds, our studies have been extended to an investigation of the effect on pepsin of another reagent with similar properties, namely guanidine hydrochloride. Although high concentrations of this reagent cause an irreversible loss of the proteolytic activity, its effects on the protein differ somewhat from those of urea and will, therefore, be presented in this report.
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 235 شماره
صفحات -
تاریخ انتشار 1960