Adenosine deaminase from human thyroid purification and some properties.
Gel filtration of human thyroid extract with Sephadex G-200 revealed two molecular forms of adenosine deaminase differing in their molecular sizes. The smaller form of adenosine deaminase was purified over 120-fold by precipitation of the protein impurities at pH5.6 and chromatography on DEAE-Sephadex A-50, Sephadex G-100 and adenosine-Sepharose. The purified enzyme was specific towards adenosine. The Michaelis constant was 5.2 X 10(-5) M. The optimum pH was about 7.0 and molecular weight 42000.
D000243:Adenosine Deaminase / Q000302:isolation & purification* / Q000378:metabolism*; D000818:Animals; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006042:Goiter / Q000201:enzymology / Q000601:surgery; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008970:Molecular Weight; D013379:Substrate Specificity; D013552:Swine; D013961:Thyroid Gland / Q000201:enzymology*
D007527:Isoenzymes; D000243:Adenosine Deaminase