Yamaguchi N, Chung S M, Ashihara T, Kawai K
Department of Preventive Medicine, Kyoto Prefectural University of Medicine, Japan.
Pancreas. 1988;3(2):207-12. doi: 10.1097/00006676-198804000-00016.
Two types of pancreatic gamma-glutamyltranspeptidase (GGTP) (EC 2.3.2.2), sialic acid poor and sialic acid rich, were purified by the following: anion-exchange chromatography, wheat germ agglutinin (WGA)-Sepharose chromatography, gel filtration chromatography, phenyl-Superose chromatography, and hydroxylapatite chromatography. Among these, WGA-Sepharose chromatography helped to increase the specific activity of the GGTPs by approximately 20-30-fold in one effort. On dodecyl sulfate polyacrylamide gel electrophoresis, the two pancreatic GGTPs had different molecular weights. Sialic acid-rich GGTP had two subunits of Mr 67,000 and 27,000; however, the sialic acid-poor type had two subunits of Mr 72,000 and 29,000. The pI value of the sialic acid-poor GGTP was 5.9, and that of the sialic acid-rich GGTP 3.6.
通过以下方法纯化了两种类型的胰腺γ-谷氨酰转肽酶（GGTP）（EC 2.3.2.2），即低唾液酸型和高唾液酸型：阴离子交换色谱法、麦胚凝集素（WGA）-琼脂糖凝胶色谱法、凝胶过滤色谱法、苯基-Superose色谱法和羟基磷灰石色谱法。其中，WGA-琼脂糖凝胶色谱法一次就使GGTP的比活性提高了约20 - 30倍。在十二烷基硫酸钠聚丙烯酰胺凝胶电泳中，两种胰腺GGTP的分子量不同。高唾液酸型GGTP有两个亚基，分子量分别为67,000和27,000；然而，低唾液酸型有两个亚基，分子量分别为72,000和29,000。低唾液酸型GGTP的pI值为5.9，高唾液酸型GGTP的pI值为3.6。
