Lee K N, Birckbichler P J, Fesus L
Prep Biochem. 1986;16(4):321-35. doi: 10.1080/00327488608068752.
Human erythrocyte transglutaminase was purified using a reusable immunoaffinity column prepared from a monoclonal antibody described previously (Birckbichler et al., Hybridoma, 4, 179-186, 1985). The purified TGase was catalytically active and exhibited a single band of apparent Mr = 85,000 on SDS-PAGE and Western blotting. The amino acid composition of the enzyme was determined. The amino terminus was blocked, and the carboxy-terminal residue appeared to be isoleucine.
使用由先前描述的单克隆抗体制备的可重复使用的免疫亲和柱纯化人红细胞转谷氨酰胺酶（Birckbichler等人，《杂交瘤》，4，179 - 186，1985年）。纯化的转谷氨酰胺酶具有催化活性，在SDS - 聚丙烯酰胺凝胶电泳和蛋白质免疫印迹分析中呈现出一条表观分子量为85,000的条带。测定了该酶的氨基酸组成。氨基末端被封闭，羧基末端残基似乎是异亮氨酸。
