Multiple forms of human adenosine deaminase: I. Purification and characterization of two molecular species
作者： Hitoshi Akedo , Hiromu Nishihara , Kiyoko Shinkai , Keiko Komatsu , Satsuki Ishikawa
DOI: 10.1016/0005-2744(72)90028-9
关键词: Sephadex 、 Chromatography 、 Size-exclusion chromatography 、 Enzyme 、 Centrifugation 、 Adenosine deaminase 、 Molecular mass 、 Biology 、 Guanidine 、 Adenosine 、 Biochemistry
摘要: Abstract 1. Gel filtration of human tissue extracts with Sephadex G-200 revealed the existence two molecular species adenosine deaminase (adenosine aminohydrolase, EC 3.5.4.4) differing markedly in their sizes. 2. Tissue-specific distributions these were also revealed. 3. The larger and smaller enzymes purified more than 1000-fold, nearly to homogeneity, from lung stomach, respectively. 4. Determination weights using a calibrated column resulted values 230 000 47 000, which reasonable accordance obtained by sucrose density gradient centrifugation. 5. No significant differences observed enzymically or immunologically between properties except for heat-stabilities activities. 6. A reversible conversion was demonstrated when former treated guanidine. 7. enzyme apparently converted after incubating sample crude supernatant. 8. possible structural relationship is discussed.
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