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At least 649 records · Page 36Linked to original sources
PubMed1985

Detection of a catalytic intermediate of peroxidase in hog thyroid microsomes.

A catalytic intermediate, Compound II of peroxidase was detected spectrophotometrically in thyroid microsomes. From comparison with the spectral data on purified thyroid peroxidase, the content of the peroxidase was estimated to be 0.019 nmol per mg of the microsomal protein, being about one-eighth of the amount of cytochrome b5. It was concluded that thyroid peroxidase exhibits the same peroxidase activity for guaiacol or ascorbate in the free and the microsome-bound forms.

Animals↗
PubMed1984

Effect of 2'-carboxymethoxy-4,4'-bis(3-methyl-2-butenyloxy)chalcone (SU-88) on prostaglandin metabolism in hog gastric mucosa.

SU-88 [2'-carboxymethoxy-4,4'-bis(3-methyl-2-butenyloxy)chalcone] inhibited the activity of the prostaglandin (PG)-metabolizing enzyme, 15-hydroxy-PG-dehydrogenase (15-OH-PG-DH), in a cytoplasmic fraction of gastric mucosa. This compound had no effect on the PG synthetase of bovine seminal vesicle microsomes and lactate dehydrogenase in rat liver. The 15-OH-PG-DH activity of gastric mucosa was not influenced by a specific inhibitor of alcohol dehydrogenase, 4-methylpyrazole. Carbenoxolone (CBX) also inhibited 15-OH-PG-DH activity. The IC50 values for SU-88 and CBX were approximately 20 and 40 microM respectively. SU-88 inhibited 15-OH-PG-DH activity uncompetitively or competitively according to whether PGE1 or NAD was used as substrate. CBX inhibited competitively the activity of this enzyme for both substrates. After the addition of SU-88 or CBX to the incubation medium of gastric mucosa, the PGE2 level of the medium was increased significantly while that of the tissue remained unchanged. These results indicate that SU-88 specifically inhibited 15-OH-PG-DH activity and suggest that 15-OH-PG-DH activity regulates the level of PGs in gastric mucosa and may have an anti-ulcer influence.

Animals↗