Abstract
Transglutaminase (TGases) are Ca2+-dependent enzymes, which link peptide-bound glutamine to primary amines. We found that wheat gliadins, purified A-gliadin and their derived peptic-tryptic peptides are effective acyl donor substrate for: 1) TGase purified from guinea pig liver 2) TGase activity of rat small intestine, measured both in jejunum slices and in influx chambers, in which only the jejunal mucosa was exposed to the substrates. The enzyme activity in jejunal mucosa homogenate, expressed as pmol of spermidine incorporated into N,N-dimethylated casein/mg/hour, is low at birth (0.10±0.02,mean±SD), increases up to 0.31±0.065 at 7-10 days and then decreases to the adult level (0.09+0.03) at 15 days of age. On the contrary, the enzyme activity of submucosa+serosa is from the 7th day at values similar to that of the adult intestine (0.5 and 0.8 respectively). 50% of TGase activity was detected in the particulate fraction (not containing brush border membranes) of both young and adult rat mucosa. These results are consistent with the hypothesis that TGase activities may be involved in the metabolism of gliadins, or of their peptides, in the lumen or in the mucosa. The specific cellular localization of the enzyme should be clarified.
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Centile, V., Esposito, C., Porta, P. et al. 41. ARE SOLUBLE AND/OR MEMBRANE-BOUND TRANSCLUTAMINASE ACTIVITIES INVOLVED IN INTESTINAL METABOLISM OF CLIADINS?. Pediatr Res 22, 103 (1987). https://doi.org/10.1203/00006450-198707000-00062
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DOI: https://doi.org/10.1203/00006450-198707000-00062