Literature DB >> 2869129

Similarity in the aldehyde oxidases from guinea-pig liver and polymorphonuclear leucocytes.

C Beedham.   

Abstract

Partially purified enzyme from guinea-pig leucocytes has been shown to have properties similar to both guinea-pig and rabbit liver aldehyde oxidase. The presence of molybdenum in the leucocyte enzyme has been demonstrated and substrate oxidation by either guinea-pig enzyme was found to be completely inhibited by menadione, a potent inhibitor of rabbit liver aldehyde oxidase. The leucocyte enzyme resembles the guinea-pig liver enzyme in terms of substrate specificity but there is considerable variation in substrate oxidation rates between the two species.

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Year:  1986        PMID: 2869129     DOI: 10.1111/j.2042-7158.1986.tb04468.x

Source DB:  PubMed          Journal:  J Pharm Pharmacol        ISSN: 0022-3573            Impact factor:   3.765


  2 in total

1.  Tissue distribution of the molybdenum hydroxylases, aldehyde oxidase and xanthine oxidase, in male and female guinea pigs.

Authors:  C Beedham; S E Bruce; D J Rance
Journal:  Eur J Drug Metab Pharmacokinet       Date:  1987 Oct-Dec       Impact factor: 2.441

2.  Breed and adaptive response modulate bovine peripheral blood cells' transcriptome.

Authors:  Nataliya Pošćić; Tommaso Montanari; Mariasilvia D'Andrea; Danilo Licastro; Fabio Pilla; Paolo Ajmone-Marsan; Andrea Minuti; Sandy Sgorlon
Journal:  J Anim Sci Biotechnol       Date:  2017-01-25
  2 in total

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