- Volume 26 Issue 5
Purification and Characterization of Aryl Acylamidase from Pseudomonas sp.
Pseudomonas sp. Aryl Acylamidase의 정제 및 성질
Aryl acylamidase [EC 220.127.116.11] present in an acetaminophen-assimilating Pseudomonas sp. has been purified to a homogeneity using series of ammonium sulfate fractionation, DEAE-Sephacel anion exchange, Phenyl-Sepharose CL-4B hydrophobic, and Sephadex G-100 gel-permeation chromatography. The molecular weight, which was estimated by gel-permeation filtration and sodium dodecyl sulfate polyacylamide gel electrophoresis, was about 57 kDa and 56 kDa, respectively, indicating that this enzyme is a monomeric protein. The optimum pH was 10.5 and the optimum temperature was 40
Acetaminophen 자화성 Pseudomonas sp.에 존재하는 aryl acylamidase[EC 18.104.22.168]는 ammonium sulfate fractionation, DEAE-Sephacel anion exchange chromatography, Phenyl-Sepharose CL-4B hydrophobic interaction chroamtography 및 Sephadex G-100 gel-permeation chromatography를 통해 순수 정제되었다. 정제된 효소는 SDS-PAGE상에서 분자량을 측정한 결과 56 kDa, Sephadex G-100 gel-permeation chromatography로 측정한 결과 57 kDa이었으며, 따라서 단일한 subunit로 구성된 효소이었다. 정제된 효소의 최대 활성을 위한 pH와 온도는 각각 pH 10.5와 4