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Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite.

Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Research Abstract Details 

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  • Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Abstract Text:

    Mice were injected with either SnCl2 (intraperitoneal) or Na2SeO3 (subcutaneous) alone or together at doses of 50 mumol/kg body weight. After 20 hours blood was collected and the concentrations of tin (Sn) and Selenium (Se) and the activity of 5-aminolaevulinate hydrolyase (ALA dehydratase, EC 4.2.1.24) in blood were determined. The concentrations of Sn in whole blood were 4.9 (SD 1.5) nmol/ml (n = 4) and ALA dehydratase activity was 10% of the control in Sn treated animals. Concentrations of Sn were 2.6 (SD 0.6) nmol/ml and ALA dehydratase activity was 92% of that in control animals when Sn and Se were simultaneously injected. The supernatant from lysed erythrocytes from Sn treated mice were applied to a Sephacryl S-300 column. The predominant peak containing Sn was eluted at the position of haemoglobin; a second peak was eluted at the position of ALA dehydratase. When the supernatant of lysed erythrocytes from mice injected with Sn and Se was chromatographed, a negligible amount of Sn was detected in the ALA dehydratase fraction. It thus appears that Sn binds to ALA dehydratase molecules and inhibits enzyme activity, and that simultaneous injection of Se prevents Sn binding to ALA dehydratase, thereby preventing the inhibition of ALA dehydratase activity by Sn.

    Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Publishing Authors By Initials

    For similar inorganic chemicals: tin compounds research abstracts see: inorganic chemicals: tin compounds research

    PUBMED ID PMID:

    MEDLINE DATE:

    Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: British journal of industrial medicine

    VOLUME: 49

    Page Numbers: 355-8

    Journal Abbreviation: Br J Ind Med

    ISSN: 0007-1072

    DAY: 28

    MONTH: May

    YEAR: 1992

    Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 370637

    Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Keywords Mesh Terms:

    KEYWORDS: Tin Compounds

    MESH TERMS: toxicity

    Chemical & Substance for Abstract: Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite. Information

    Substance Name: Porphobilinogen Synthase

    Registry Number: EC 4.2.1.24

    Grant and Affiliation Information for Inhibition of erythrocyte 5-aminolaevulinate hydrolase activity by tin and its prevention by selenite.

    AFFILIATION: Department of Hygiene, Juntendo University School of Medicine, Tokyo, Japan.

    Country: ENGLAND

    ENGLAND Research PublicationENGLAND Research Publication

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    MEDLINETA: Br J Ind Med

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