title: Preparative purification of adenosine deaminase from human erythrocytes by affinity chromatography.
abstract: The purification of adenosine deaminase from human erythrocytes is reported. By means of classical procedures and by using affinity chromatography as the last step, the enzyme is purified 760,000-fold with a yield of 32%. The affinity resin is composed of purine riboside (nebularine) linked to Sepharose CL6B. Since the compound has no leaving group at the C-6 position the affinity gel is stable and the chromatography can be repeated several times (up to fifteen times in eight months). Purine riboside was chosen because its potency as a reversible inhibitor of adenosine deaminase is greater than that of inosine (a low-affinity inhibitor), but lower than that of erythro-9-(2-hydroxy-3-nonyl)adenine (a high-affinity inhibitor).
authors.affiliation: Departament de Bioquimica i Fisiologia, Facultat de Quimica, Universitat de Barcelona, Catalunya, Spain.
authors.forename: J M
authors.initials: JM
authors.lastname: Aran
authors.forename: E I
authors.initials: EI
authors.lastname: Canela
authors.forename: R
authors.initials: R
authors.lastname: Franco
mesh_terms: D000243:Adenosine Deaminase / Q000097:blood*; D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000201:enzymology*; D006801:Humans; D007527:Isoenzymes / Q000097:blood*; D008970:Molecular Weight; D011684:Purine Nucleosides; D012263:Ribonucleosides; D012685:Sepharose
chemical_list: D007527:Isoenzymes; D011684:Purine Nucleosides; D012263:Ribonucleosides; D012685:Sepharose; C005248:nebularine; D000243:Adenosine Deaminase