Literature DB >> 3803347

Nonspecific snail muscle adenylate deaminase: simplified purification, characterization and use for the preparation of deamino derivatives of NAD, NADH and AMP-P(NH)P.

A J Stankiewicz.   

Abstract

Chromatography on phosphocellulose P-11 under conditions different from those applicable for deaminases specific to 5' AMP resulted in homogeneous preparation of snail foot muscle enzyme. Snail deaminase is a tetramer with molecular weight of 240,000, composed of four apparently identical subunits. Its amino acid composition is remarkably different from deaminases of higher animals, it was not inhibited by EDTA, but zinc became inhibitory to the snail enzyme. Unlike deaminases specific to 5' AMP, nonspecific deaminase is not a zinc-containing enzyme. It was adopted further for the preparation of hypoxanthine derivatives of adenosine-containing nucleotides such as NAD, NADH, AMP-P(NH)P, AMP, ADP and ATP.

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Year:  1986        PMID: 3803347     DOI: 10.1159/000469291

Source DB:  PubMed          Journal:  Enzyme        ISSN: 0013-9432


  1 in total

1.  Partial characterization of the gene encoding myoadenylate deaminase from the teleost fish Platichthys flesus.

Authors:  M T Thébault; A Tanguy; A L Meistertzheim; J P Raffin
Journal:  Fish Physiol Biochem       Date:  2009-10-11       Impact factor: 2.794

  1 in total

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