R. Quezadacalvillo et al., MURINE INTESTINAL DISACCHARIDASES - IDENTIFICATION OF STRUCTURAL VARIANTS OF SUCRASE-ISOMALTASE COMPLEX, The American journal of physiology, 265(6), 1993, pp. 70001141-70001149
This study was directed to determine the extent of variability in stru
cture or expression of intestinal disaccharidases [gamma-glucoamylase
(gamma-GA), sucrase-isomaltase (SI), and lactase] between different st
rains of mice. Reduced levels of sucrase activity (approximately 20 U/
g of protein) were observed in three strains of mice belonging to the
CBA/Ca lineage. Four other strains of mice analyzed exhibited higher l
evels of sucrase activity (approximately 50 U/g of protein). Decreased
levels of sucrase in CBA/Ca mice were not associated with decreased l
evels of activity associated with the isomaltase subunit or with decre
ased levels of SI mRNA expression. High-performance liquid chromatogra
phic gel filtration, heat inactivation, and kinetic analysis indicated
that the differences between strains in sucrase activity might be att
ributed to structural differences in the sucrase subunit of the SI com
plex, thus rendering it more susceptible to cleavage and inactivation.
However, no differences in kinetic properties of the sucrase subunit
were observed between strains. Murine gamma-GA was found to account fo
r a greater proportion of maltase activity (approximately 70 %) than t
hat observed in other species (i.e., approximately 20%). In addition,
CBA/Ca mice were found to be deficient in intestinal maltase activity
(approximately 60 U/g) compared with the other strains studied (approx
imately 300 U/g).