PMID: 70224Aug 11, 1977Paper

Immunochemical studies on the subunits of rabbit-intestinal sucrase-isomaltase complex

Biochimica Et Biophysica Acta
Y TakesueY Nishi

Abstract

Purified sucrase-isomaltase complex sucrose alpha-glucohydrolase, EC 3.2.1.48 - dextrin 6-alpha-glycanohydrolase, EC 3.2.1.10) solubilized by papain from rabbit intestine was dissociated by citraconylation into its subunits, sucrase and isomaltase, which were then isolated in a form active immunologically as well as enzymatically by affinity chromatography on Sephadex G-200 and gel-filtration on Bio-gel P-300. Antibodies against the purified complex inhibited isomaltase but not sucrase and formed precipitation lines, crossing each other, with isolated sucrase and isomaltase, showing that the two enzymes differ in antigenicity from each other. By absorbing the antibodies with isolated sucrase and isomaltase, antibodies specific for isomaltase and sucrase, respectively, were obtained. Like the original antibodies, both of the specific antibodies quantitatively agglutinated microvillous vesicles. Sucrase was inhibited by neither of the antibodies. In contrast, isomaltase was greatly inhibited by the isomaltase-specific antibodies, but not by the sucrase-specific ones.

References

Jan 6, 1970·Biochimica Et Biophysica Acta·R GitzelmannG Semenza
Jan 1, 1968·Analytical Biochemistry·A Dahlqvist
Mar 1, 1969·Journal of Biochemistry·Y Takesue, T Kashiwagi
Apr 1, 1969·Journal of Biochemistry·Y Takesue

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Citations

Nov 1, 1992·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·K YokotaY Takesue
Jan 1, 1978·Journal of Ultrastructure Research·Y Nishi, Y Takesue

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