Evangelista M, Chersi A, Citro G
Laboratory of Biochemistry, Regina Elena Institute for Cancer Research, Rome, Italy.
Biochim Biophys Acta. 1991 May 24;1074(1):214-6. doi: 10.1016/0304-4165(91)90064-n.
Antibodies were raised in a rabbit by using a 12-residue synthetic peptide, corresponding to fragment 2-13 of rat placental glutathione S-transferase, as the immunogen. The antiserum appeared to react with the fragment as well as with the corresponding human enzyme (GST-pi), which shares with the rat transferase a 92% sequence homology at the N terminus. In addition, the binding of the antibody to the protein was completely inhibited by small amounts of peptide. The enzymatic activity of glutathione transferase was not affected by the antibody. This might indicate that the N-terminal fragment is not involved in the catalytic activity of the enzyme. This antibody of predetermined specificity might thus find a useful application for the detection and approximate quantitation of this marker in human preneoplastic lesions.
通过使用一段12个氨基酸残基的合成肽（对应大鼠胎盘谷胱甘肽S-转移酶的2-13片段）作为免疫原，在兔子体内产生了抗体。抗血清似乎既能与该片段反应，也能与相应的人类酶（GST-pi）反应，后者与大鼠转移酶在N端有92%的序列同源性。此外，少量的肽完全抑制了抗体与该蛋白质的结合。谷胱甘肽转移酶的酶活性不受抗体影响。这可能表明N端片段不参与该酶的催化活性。因此，这种具有预定特异性的抗体可能在检测和大致定量人类癌前病变中的这种标志物方面找到有用的应用。
