Literature DB >> 12381379

Characterization and purification of adenosine deaminase 1 from human and chicken liver.

Sachiko Iwaki-Egawa1, Yasuhiro Watanabe.   

Abstract

Adenosine deaminase 1 (ADA1) was purified from human and chicken liver. The purified enzyme had a molecular weight of approximately 42,000 Da on SDS-PAGE. In humans, ADA1 was mainly purified concomitant with ADA-binding protein, dipeptidyl peptidase IV (DPP IV)/CD26; however, in chickens, only ADA1 without DPP IV was purified. Both human and chicken ADA1s showed similar properties on substrate specificities, sensitivities on inhibitors, and pH profile. However, they had different affinities with adenosine-Sepharose and IgG anti-ADA1-Sepharose. Human ADA1 was not adsorbed in adenosine-Sepharose column, but chicken ADA1 was adsorbed. As for IgG anti-ADA1-Sepharose column, the results were converse. Furthermore, human ADA1 could bind to DPP IV whereas chicken ADA1 could not.

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Year:  2002        PMID: 12381379     DOI: 10.1016/s1096-4959(02)00122-7

Source DB:  PubMed          Journal:  Comp Biochem Physiol B Biochem Mol Biol        ISSN: 1096-4959            Impact factor:   2.231


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  3 in total

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