Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In the paper we observed histochemically the distribution and activity of 16 enzymes in the normal rat gastric mucosa. The lysosomal enzymes were demonstrated by the method of semipermeable membranes (LOJDA 1972). At the proof of dehydrogenases aqueous and gel media were used. The parietal cells of the gastric mucosa contained a moderate activity of acid phosphatase, E-600 resistant esterase, and only a very slight activity of beta-glucuronidase and N-acetyl-beta-D-glucosaminidase. The macrophages of the interstice contained a high activity of beta-glucruonidase, acid phosphatase, E-600 resistant esterase and a low activity of N-acetyl-beta-D-glucosaminidase. The chief cells of the rat gastric mucosa, in contrast to the human, did not contain nonspecific esterase and also in them acid phosphatase was mostly lacking. The alkaline phosphatase was found only in the endothelium of the capillaries of the gastric mucosa. The parietal cells contained high activities of succinate dehydrogenase, alpha-glycerophosphate dehydrogenase, beta-hydroxybutyrate dehydrogenase, NADH tetrazolium reductase, a lower activity of NADPH tetrazolium reductase, as well as other soluable dehydrogenases. At the examination of dehydrogenases using aqueous as well as gel media with PMS during optimal short incubation periods, we found more and less active forms of parietal cells. The different oxidoreductase capacity of parietal cells in normal rat gastric mucosa can point to their unequal-functional load at the production of hydrochloric acid. The findings obtained are compared with the findings in older papers concerning different experimental animals and with the distribution of enzymes in the human gastric mucosa.
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PMID:Histochemical localization of enzymes in the normal rat gastric mucosa using the technique of the semipermeable membranes and the other methods. 82 7

The influence of starving on the activity of enzymes of the rat gastric mucosa was investigated by selected histochemical methods. Beside the conventional methods of enzymatic histochemistry the technique of semipermeable membranes was used in the proof of lysosomal enzymes. Dehydrogenases were proved in aqueous and also in gel media with PMS. During the starvation in the parietal cells a marked increase took place in the activity of acid phosphatase, E-600 resistant esterase, less in beta-glucuronidase. High activity of the lysosomal enzymes in macrophages did not change during starvation. Nor did any changes took place in the activity of alkaline phosphatase in the endothelium of the capillaries. The chief cells in the control and starving animals, in contrast to the human gastric mucosa, did not contain any non-specific esterase. Concerning dehydrogenases, parietal cells with a different activity of these enzymes were observed both in starved and control animals. In the rat gastric mucosa starving induced changes in the activity of the enzymes which mark important organelles of the cells. Thus it is possible to consider the observed histochemical changes as a functional manifestation of morphological damage of cellular structures which are affected during starvation.
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PMID:Histochemical findings in the rat gastric mucosa during starvation. 99 73