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Biomedical subjects

O Wada

Publications and source records attributed to O Wada.

At least 181 records · Page 10Linked to original sources
PubMed1977

[Aspects of enzymatic toxicology of metals. A review (author's transl)].

The adverse and beneficial effects of metals have occupied a great concern in many branches of biology for centuries, but their biochemical roles have been studied systematically only in the last four decades. Almost all the metals, especially those of high toxicity, bind readily to mercapto groups, and these are frequently important in enzyme systems. Furthermore, a large number of in vitro and in vivo studies have shown that toxic metals can replace essential metals in many of their metalloenzymes, with resultant changes in activity. Metals also bind to protein, phospholipid and nucleic acid, and have been shown to effect a change in the conformation of enzymes required for normal function, or to uncouple oxidative phosphorylation. This review, of necessity brief, will focus on the biochemical and enzymatic effects of metals, emphasizing meanings available to occupational medicine. The present knowledge on enzymatic toxicology of metals can provide for access to three main problems. These include an exposure evaluation, a health injury evaluation and a pathogenic understanding of workers exposed to metals. In this article, these problems are discussed in general, and the recent developments made in the enzymatic toxicology of cadmium and lead are presented with pertinent literatures.

Alanine Transaminase↗
PubMed1974

Measurement of delta-aminolevulinic acid synthetase activity in human erythroblasts.

A new, specific, and simple method for the determination of delta-aminolevulinic acid (ALA) synthetase activity in human bone marrow cells has been developed. ALA synthetase of erythroblasts was partially purified so as to permit the use of [(14)C]succinyl-CoA as a substrate for this enzyme. In this enzyme preparation there were negligible activities of succinyl-CoA hydrolase, alpha-ketoglutarate dehydrogenase, and succinyl-CoA synthetase and there was no activity of ALA dehydrase. The ALA formed from [(14)C]succinyl-CoA has been isolated by column chromatography. Radioactivity in the eluate from the column has been proved by paper chromatography to be exclusively that of [(14)C]ALA. The entire assay can be completed within 4 h, and [(14)C]succinyl-CoA was incorporated into [(14)C]ALA on the order of several percent. Moderate to marked decreases of ALA synthetase activity have been demonstrated in the erythroblasts of all cases of sideroblastic anemia. In the cases of iron deficiency anemia, on the other hand, normal or slightly elevated activity has been obtained.

5-Aminolevulinate Synthetase↗