Isoenzymatic forms of human cytidine deaminase.
Protein Eng Des Sel
; 17(12): 871-7, 2004 Dec.
Article
en En
| MEDLINE
| ID: mdl-15713780
Cytidine deaminase (CDA) purified from human placenta revealed the presence of five isoenzymatic forms that differ only in their isoelectric point. Since human cytidine deaminase exists in two variants (CDA 1 and CDA 2) with a non-conservative amino acid substitution at codon 27, in this work we demonstrate that these two variants may combine together in vitro, giving five CDA isoforms as observed in vivo from human placenta. For this purpose, each of the two forms of CDA was purified close to homogeneity and dissociated into monomers in the presence of a small amount of sodium dodecyl sulfate as a dissociating agent. The monomers were mixed together and subjected to anion-exchange chromatography and to chromatofocusing analysis in order to visualize the formation of the five isoforms. Furthermore, for both CDA 1 and CDA 2 some substrates and inhibitors of CDA were assayed, with the aim of demonstrating different kinetic behavior between the two natural variants.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Citidina Desaminasa
Límite:
Humans
Idioma:
En
Revista:
Protein Eng Des Sel
Asunto de la revista:
BIOQUIMICA
/
BIOTECNOLOGIA
Año:
2004
Tipo del documento:
Article
País de afiliación:
Italia
Pais de publicación:
Reino Unido