Results 91 to 100 of about 1,571 (110)

Diet management in congenital diarrheas and enteropathies - general concepts and disease-specific approach, a narrative review. [PDF]

open access: yesAm J Clin Nutr
Avitzur Y   +12 more
europepmc   +1 more source

In vitro and in silico studies and a systematic literature review of antiglycation properties of amlodipine. [PDF]

open access: yesSci Rep
Dańkowska K   +8 more
europepmc   +1 more source

Salmonella infection accelerates postnatal maturation of the intestinal epithelium. [PDF]

open access: yesProc Natl Acad Sci U S A
Schlößer S   +20 more
europepmc   +1 more source

Paediatric Intestinal Enteroids Derived from Very Early Onset Inflammatory Bowel Disease Reveal Differences in Growth, Morphology, and Barrier Function

open access: yes
Balakrishnan V   +10 more
europepmc   +1 more source

A hydrophobic form of the small-intestinal sucrase-isomaltase complex

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1975
A large scale preparation of brush border membranes is described. Solubilized by either papain or Triton X-100, the sucrase-isomaltase complex is purified in a three-step procedure, including differential centrifugation, Sephadex G-200 and DEAE-cellulose chromatography.
H, Sigrist, P, Ronner, G, Semenza
openaire   +2 more sources

Murine intestinal disaccharidases: identification of structural variants of sucrase-isomaltase complex

American Journal of Physiology-Gastrointestinal and Liver Physiology, 1993
This study was directed to determine the extent of variability in structure or expression of intestinal disaccharidase [gamma-glucoamylase (gamma-GA), sucrase-isomaltase (SI), and lactase] between different strains of mice. Reduced levels of sucrase activity (approximately 20 U/g of protein) were observed in three strains of mice belonging to the CBA ...
R, Quezada-Calvillo   +3 more
openaire   +2 more sources

Hydrodynamic Properties of the Sucrase Isomaltase Complex from Rabbit Small Intestine

European Journal of Biochemistry, 1973
From the hydrodynamic properties of the sucrase · isomaltase complex at low ionic strength, a molecular weight of 221000 was calculated. The complex dimerizes at high ionic strength. Under denaturing conditions the complex dissociates into two subunits of identical or almost identical molecular weight (112000) which are presumably composed of one ...
H, Mosimann, G, Semenza, H, Sund
openaire   +2 more sources

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

Biochimica et Biophysica Acta (BBA) - Enzymology, 1977
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 ...
Y, Takesue, R, Tamura, Y, Nishi
openaire   +2 more sources

Tryptic Digestion of Native Small‐Intestinal Sucrase · Isomaltase Complex: Isolation of the Sucrase Subunit

European Journal of Biochemistry, 1975
Limited tryptic digestion of native sucrase · isomaltase complex produced a more rapid destruction of isomaltase activity than sucrase activity. It was possible to isolate a partially fragmented sucrase subunit in high yields with a specific activity twice that of the native complex.
A, Quaroni   +2 more
openaire   +2 more sources

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