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Am J Physiol Gastrointest Liver Physiol 265: G1150-G1157, 1993;
0193-1857/93 $5.00
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AJP - Gastrointestinal and Liver Physiology, Vol 265, Issue 6 1150-G1157, Copyright © 1993 by American Physiological Society

ARTICLES

Characterization of intestinal gamma-glucoamylase deficiency in CBA/Ca mice

R. Quezada-Calvillo, M. Senchyna and B. J. Underdown
Department of Pathology, McMaster University, Hamilton, Ontario, Canada.

In previous work, we found that CBA/Ca mice display only 20% of the maltase activity present in other mouse strains. In this study, we characterized more fully the maltase deficiency in CBA/Ca mice. Virtually all of the intestinal maltase activity of CBA/Ca mice was inactivated at 50 degrees C, indicating that it was due only to the sucrase-isomaltase complex. High-performance liquid chromatographic analysis revealed that CBA/Ca mice had undetectable maltase activity displaying the molecular mass characteristic of murine gamma-glucoamylase (gamma-GA) (530 kDa). Gel electrophoretic analysis confirmed that CBA/Ca mice lacked maltase activity with molecular mass of 530 kDa corresponding to gamma-GA. Two-dimensional electrophoretic analysis revealed that the gamma-GA deficiency in CBA/Ca mice was due to the failure to synthesize the enzyme and not to the synthesis of an inactive protein. gamma-GA maltase activity could not be induced in CBA/Ca mice by a diet rich in starch, whereas the activity of other disaccharidases were readily increased. gamma-GA-deficient CBA/Ca mice appear to lack any gross metabolic abnormality resulting from this defect.


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B. L. Nichols, J. Eldering, S. Avery, D. Hahn, A. Quaroni, and E. Sterchi
Human Small Intestinal Maltase-glucoamylase cDNA Cloning. HOMOLOGY TO SUCRASE-ISOMALTASE
J. Biol. Chem., January 30, 1998; 273(5): 3076 - 3081.
[Abstract] [Full Text] [PDF]


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