Alin P, Mannervik B, Jörnvall H
FEBS Lett. 1985 Mar 25;182(2):319-22. doi: 10.1016/0014-5793(85)80324-0.
Cytosolic glutathione transferase was purified from human placenta and human liver. Three different forms of the enzyme were obtained, the acidic (pi), the near-neutral (mu), and the basic (alpha-epsilon) forms; two had free alpha-amino groups (pi, mu) and one had a blocked alpha-amino group (alpha-epsilon). N-terminal sequence analyses and total compositions gave clearly different results for each form, although transferases pi and mu showed 35% sequence homology in the N-terminal regions, with a 1-residue shift in starting position. Consequently, the proteins are concluded to be products of three discrete but related genes.
胞质谷胱甘肽转移酶从人胎盘和人肝脏中纯化得到。获得了该酶的三种不同形式，即酸性（π）、近中性（μ）和碱性（α-ε）形式；两种具有游离α-氨基（π、μ），一种具有封闭的α-氨基（α-ε）。尽管转移酶π和μ在N端区域显示出35%的序列同源性，但起始位置有1个残基的位移，每种形式的N端序列分析和总组成给出了明显不同的结果。因此，得出这些蛋白质是三个不连续但相关基因的产物的结论。
