Gopalan P, Jensen D E, Lotlikar P D
Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA.
Cancer Lett. 1992 Jul 10;64(3):225-33. doi: 10.1016/0304-3835(92)90047-y.
Glutathione (GSH) conjugation of microsome-mediated and synthetic aflatoxin B1 (AFB1)-epoxide and styrene oxide has been investigated with purified GSH S-transferases (GSTs) from rats. Both styrene oxide and AFB1-epoxide were conjugated preferentially by millimicrons GSTs 3-3, 3-4 and 4-4 as compared to alpha GSTs 1-1, 1-2 and 2-2. The highest catalytic activity with styrene oxide conjugation was associated with GST 4-4. The highest catalytic activity with microsome-mediated AFB1-epoxide conjugation was observed with GST 3-3 whereas with the synthetic AFB1-epoxide conjugation was seen with GST 4-4. The catalytic activity of pi GST 7-7 was intermediate to millimicrons and alpha GSTs. It is suggested that GST 3-3 may play an important role in inactivation of AFB1-epoxide generated in vivo in the rat.
已用从大鼠中纯化得到的谷胱甘肽S-转移酶（GSTs）研究了微粒体介导的以及合成的黄曲霉毒素B1（AFB1）-环氧化物和苯乙烯氧化物与谷胱甘肽（GSH）的结合作用。与α GSTs 1-1、1-2和2-2相比，苯乙烯氧化物和AFB1-环氧化物均优先被毫微摩尔GSTs 3-3、3-4和4-4结合。与苯乙烯氧化物结合的最高催化活性与GST 4-4相关。在微粒体介导的AFB1-环氧化物结合中，观察到GST 3-3具有最高催化活性，而在合成的AFB1-环氧化物结合中，GST 4-4具有最高催化活性。π GST 7-7的催化活性介于毫微摩尔GSTs和α GSTs之间。有人提出，GST 3-3可能在大鼠体内生成的AFB1-环氧化物的失活过程中起重要作用。
