Studies on the structure and function of muscle aldolase. IV. The action of dilute alkali on primary structure and its effect on the determination of subunit molecular weight.
نویسندگان
چکیده
In 0.05 M potassium phosphate buffer (pH 7.0, ZO”), native rabbit muscle aldolase has been found to exhibit a molecular weight (mn N g, pZ) close to 160,000, in agreement with previous findings. Upon exposure to cold alkaline borate buffer (pH 12.5, p = 0.17, 0”), the enzyme spontaneously dissociates into its monomers which subsequently undergo slow hydrolytic degradation. Compensating for electrostatic charge effects and extrapolating the data to zero time in alkali, a subunit molecular weight of 41,400 to 42,000 is obtained. If the native enzyme is exposed to alkaline conditions at 20°, the subunits undergo an initial rapid degradation which eventually yields alkali-resistant material. Similar results are obtained with succinyl aldolase subunits under equivalent conditions. Acrylamide gel electrophoresis of alkali-treated succinyl aldolase (pH 12.5,30’) results in the appearance of a limited number of electrophoretic bands. This finding suggests that specific alkali-labile peptide bonds are involved in the degradation process. As a further consequence of the action of alkali, native aldolase shows increased solubility properties. Both native and succinyl aldolase manifest new NH&erminal serine, threonine, and glycine residues after treatment with borate buffer at pH 12.5 and 30’. Prolonged exposure to alkali results in increased liberation of the above end groups,
منابع مشابه
Studies on the Structure and Function of Muscle Aldolase IV. THE ACTION OF DILUTE ALKALI ON PRIMARY STRUCTURE AND ITS EFFECT ON THE DETERMINATION OF SUBUNIT MOLECULAR WEIGHT*
In 0.05 M potassium phosphate buffer (pH 7.0, ZO”), native rabbit muscle aldolase has been found to exhibit a molecular weight (mn N g, pZ) close to 160,000, in agreement with previous findings. Upon exposure to cold alkaline borate buffer (pH 12.5, p = 0.17, 0”), the enzyme spontaneously dissociates into its monomers which subsequently undergo slow hydrolytic degradation. Compensating for elec...
متن کاملStudies on the Structure and Function of Muscle Aldolase IV. THE ACTION OF DILUTE ALKALI ON PRIMARY STRUCTURE AND ITS EFFECT ON THE DETERMINATION OF SUBUNIT MOLECULAR WEIGHT*
In 0.05 M potassium phosphate buffer (pH 7.0, ZO”), native rabbit muscle aldolase has been found to exhibit a molecular weight (mn N g, pZ) close to 160,000, in agreement with previous findings. Upon exposure to cold alkaline borate buffer (pH 12.5, p = 0.17, 0”), the enzyme spontaneously dissociates into its monomers which subsequently undergo slow hydrolytic degradation. Compensating for elec...
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 244 2 شماره
صفحات -
تاریخ انتشار 1969