Literature DB >> 6840227

Alteration of activities of delta-aminolevulinic acid synthase, delta-aminolevulinic acid dehydratase and delta-aminolevulinic acid dehydratase inhibitor in the bone marrow cells of lead poisoned rats.

M Kondo, M Kajimoto, G Urata.   

Abstract

A new modified method for the determination of delta-aminolevulinic acid (ALA) dehydratase activity has been developed. This modified method involves addition of 0.1 mM Zn2+ and then preheating the enzyme solution at 60 degrees C for 5 min before following commonly used procedures. The ALA dehydratase activity in the peripheral blood of lead poisoned rats, determined by this procedure, was approximately 7.5-fold higher than control values. The activity of ALA dehydratase in the bone marrow cells of lead poisoned rats increased approximately 2-fold. These increases were accompanied by a simultaneous decrease in an inhibitor specific for ALA dehydratase. Consequently, these results suggest that ALA dehydratase is induced after the reduction of ALA dehydratase activity, and that ALA dehydratase activity is controlled by a new specific ALA dehydratase inhibitor.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6840227

Source DB:  PubMed          Journal:  Exp Hematol        ISSN: 0301-472X            Impact factor:   3.084


  2 in total

1.  An autopsy case of acute porphyria with a decrease of both uroporphyrinogen I synthetase and ferrochelatase activities.

Authors:  M Yamada; M Kondo; M Tanaka; R Okeda; S Hatakeyama; T Fukui; H Tsukagoshi
Journal:  Acta Neuropathol       Date:  1984       Impact factor: 17.088

2.  The effects of ethanol, estrogen, and hexachlorobenzene on the activities of hepatic delta-aminolevulinate synthetase, delta-aminolevulinate dehydratase, and uroporphyrinogen decarboxylase in male rats.

Authors:  M Kondo; Y Shimizu
Journal:  Arch Toxicol       Date:  1986-10       Impact factor: 5.153

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.