Studies on a Soluble Dipeptidase from Pig Intestinal Mucosa. Enzymatic Properties.
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چکیده
منابع مشابه
Antioxidative properties of pig vesical mucosa: a comparison with gastric and intestinal mucosa.
The antioxidative properties of pig urinary bladder mucosa were compared with those of gastric and intestinal mucosa using nitroxide radicals. Electron paramagnetic resonance (EPR) method was used to monitor the metabolic processes of nitroxides in mucosae. The reduction of nitroxides was measured on intact luminal surfaces of gastric, intestinal, and urinary bladder mucosa, as well as in homog...
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1. Rats were mated and at weekly intervals during pregnancy and lactation, and after weaning, the dipeptidase activity in the supernatant fraction from small intestinal mucosa extracts was determined for two dipeptides: glycyl-L-leucine dipeptidase (EC 3.4.3.2) AND L-alanyl-L-glutamic acid dipeptidase. 2. Dipeptidase activity is found mainly in the soluble (spernantant) fraction of the mucosa h...
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A dipeptide hydrolase from the brush border of guinea-pig intestinal mucosa was purified. The enzyme resembles another dipeptide hydrolase isolated from the cytosol fraction of intestinal mucosa. Studies on the binding of cytosol peptide hydrolase to brush-border membranes indicate that the enzyme found in the brush border may be a cytoplasmic contaminant.
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the absorption of vitamin B(12) in many animals requires its prior association with intrinsic factor (IF) and attachment to a specific receptor in the intestine. Employing Triton X-100, we have solubilized from guinea pig ileum a factor that binds intrinsic factor-vitamin B(12) complex (IF-B(12)). This binding factor was soluble to the extent that it was not sedimented by centrifugation at 100,...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1974
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.28b-0711