Federici G, Di Ilio C, Sacchetta P, Polidoro G, Bannister J V
Int J Biochem. 1985;17(5):653-6. doi: 10.1016/0020-711x(85)90300-3.
Glutathione S-transferase activity from human platelets was purified to homogeneity by affinity chromatography. The purified enzyme was found to be the acidic form and its molecular and catalytic properties were identical to acidic glutathione S-transferases purified from other human tissues. The purified platelet enzyme had no peroxidase activity and did not protect microsomes against peroxidation.
通过亲和层析将人血小板中的谷胱甘肽S-转移酶活性纯化至同质。发现纯化后的酶为酸性形式，其分子和催化特性与从其他人体组织中纯化得到的酸性谷胱甘肽S-转移酶相同。纯化后的血小板酶没有过氧化物酶活性，也不能保护微粒体免受过氧化作用。
