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Literature DB >> 5494221

The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites.

Abstract

A protein fraction was isolated from guinea-pig liver that binds triethyltin with an affinity of approx. 2x10(6)m(-1) at pH8.0. It was shown that the protein responsible for binding 70% of the triethyltin found in guinea-pig liver after injection of radioactively labelled triethyltin is at most a few per cent of the total liver protein. Evidence is presented from the kinetics of loss of binding and loss of certain amino acids on photo-oxidation with either Methylene Blue or Rose Bengal that each binding site consists of two histidine residues.

Entities: Chemical Species

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Year: 1970 PMID： 5494221 PMCID： PMC1179579 DOI： 10.1042/bj1200151

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

21 in total

2. Oxidative phosphorylation. The relation between the specific binding of trimethylytin and triethyltin to mitochondria and their effects on various mitochondrial functions.

Authors: W N Aldridge; B W Street
Journal: Biochem J Date: 1971-08 Impact factor: 3.857

3. Biochemical effects of the hypoglycaemic compound diphenyleneiodonnium. Catalysis of anion-hydroxyl ion exchange across the inner membrane of rat liver mitochondria and effects on oxygen uptake.

Authors: P C Holland; H S Sherratt
Journal: Biochem J Date: 1972-08 Impact factor: 3.857

4. Triethyltin binding to cat haemoglobin. Evidence for two chemically distinct sites and a role for both histidine and cysteine residues.

Authors: B M Elliott; W N Aldridge; J W Bridges
Journal: Biochem J Date: 1979-02-01 Impact factor: 3.857

5. Oxidative phosphorylation. The effect of anions on the inhibition by triethyltin of various mitochondrial functions, and the relationship between this inhibition and binding of triethyltin.

Authors: M S Rose; W N Aldridge
Journal: Biochem J Date: 1972-03 Impact factor: 3.857

5 in total

The interaction of triethyltin with a component of guinea-pig liver supernatant. Evidence for histidine in the binding sites.

1. Trialkyltins and oxidative phosphorylation. The [32P]phosphate-adenosine triphosphate-exchange reaction.

2. The biochemistry of organotin compounds: trialkyltins and oxidative phosphorylation.

3. The biochemistry of organo-tin compounds; diethyltin dichloride and triethyltin sulphate.

4. Photooxidation of amino acids in the presence of methylene blue.

5. Tertiary structure of ribonuclease.

6. Oxidative phosphorylation. Biochemical effects and properties of trialkyltins.

7. Ammonium sulfate concentration conversion nomograph for 0 degrees.

8. The structure of ribonuclease-S at 3.5 A resolution.

9. Oxidative phosphorylation. The specific binding of trimethyltin and triethyltin to rat liver mitochondria.

10. The interaction of triethyltin with components of animal tissues.

1. Binding of triethyltin to cat haemoglobin and modification of the binding sites by diethyl pyrocarbonate.

2. Oxidative phosphorylation. The relation between the specific binding of trimethylytin and triethyltin to mitochondria and their effects on various mitochondrial functions.

3. Biochemical effects of the hypoglycaemic compound diphenyleneiodonnium. Catalysis of anion-hydroxyl ion exchange across the inner membrane of rat liver mitochondria and effects on oxygen uptake.

4. Triethyltin binding to cat haemoglobin. Evidence for two chemically distinct sites and a role for both histidine and cysteine residues.

5. Oxidative phosphorylation. The effect of anions on the inhibition by triethyltin of various mitochondrial functions, and the relationship between this inhibition and binding of triethyltin.