title: Purification of human pancreatic gamma-glutamyltranspeptidase by lectin affinity chromatography.
abstract: 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.
mesh_terms: D002846:Chromatography, Affinity / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007525:Isoelectric Focusing; D007527:Isoenzymes; D037102:Lectins; D008970:Molecular Weight; D010179:Pancreas / Q000201:enzymology*; D012967:Sodium Dodecyl Sulfate; D005723:gamma-Glutamyltransferase / Q000302:isolation & purification*
chemical_list: D007527:Isoenzymes; D037102:Lectins; D012967:Sodium Dodecyl Sulfate; D005723:gamma-Glutamyltransferase