intestine

Type V collagen (from mouse intestine) serves as an immunization-grade protein that can elicit a specific immune response in animals, generating antibodies directed against this collagen. Additionally, this collagen functions as a hydrolytic substrate for matrix metalloproteinases (MMPs).

Tyvelose is an unusual 3,6-dideoxyhexose terminal sugar and the immunodominant component of glycoprotein antigens in the parasitic helminth T. spiralis, which is responsible for trichinosis in humans. It is produced in high amounts by the infective larva and is immunodominant during the muscle stage of infection. Mice immunized with tyvelose-BSA produce IgG1 antibodies to tyvelose but are not resistant to infection by T. spiralis. Tyvelose-specific antibodies (2.5 mg/20 g) administered to rat pups leads to expulsion of first stage larvae from the intestine within one hour.

HumanapolipoproteinAIV is a plasma protein synthesized primarily in the enterocytes of the small intestine during fat absorption. It serves as a major circulating apolipoprotein and plays a role in dietary fat absorption, triglyceride transport, and the reverse transport of cholesterol.

Trehalase, Porcine (EC 3.2.1.28), is a glycoside hydrolase enzyme found in the brush border of the small intestine, where it facilitates the conversion of trehalose into glucose.

β-Glucanase 1(thermostable) is a glucosidase located at the brush border of the small intestine, targeting β1→4 glycosidic bonds between glucose or glucose-substituted molecules (such as the disaccharide cellobiose). This enzyme is an exocellulase specific to various β-D-glycosidic substrates. It catalyzes the hydrolysis of non-reducing terminal residues of β-D-glucosides, releasing glucose.

Pancreozymin, Porcine stimulates the secretion of pancreatic enzymes from small intestine extracts.

Amyloglucosidase, Rhizopus sp. (EC 3.2.1.3), is an enzyme located at the brush border of the small intestine that hydrolyzes terminal (1→4) linked α-D-glucose residues, releasing β-D-glucose.

α-Glucosidase, Escherichia coli (EC 3.2.1.20), is a glucosidase found in the brush border of the small intestine that acts on 1,4-α-glycosidic bonds, breaking down starches and disaccharides into glucose.

β-Glucanase 2 (thermostable) is a glucosidase located at the brush border of the small intestine, acting on β1→4 glycosidic bonds connecting two glucose or substituted glucose molecules (such as disaccharide cellodextrin). It is an exocellulase with specificity for various β-D-glycoside substrates, catalyzing the hydrolysis of non-reducing terminal β-D-glucosidic residues to release glucose.

α-Glucosidase, Saccharomyces cerevisiae (EC 3.2.1.20), is an enzyme classified as a glucosidase found in the brush border of the small intestine. It acts on 1,4-α-glycosidic bonds to break down starch and disaccharides into glucose.

β-Glucosidase (thermostable) is a glucose-metabolizing enzyme found in the brush border of the small intestine, targeting the β1→4 glycosidic bonds joining two glucose or glucose-substituted molecules, such as in disaccharides like cellobiose. This enzyme functions as an exocellulase with specificity for various β-D-glycoside substrates. It facilitates the hydrolysis of terminal non-reducing residues in β-D-glucosides, resulting in the release of glucose.