Analysis of Site-specific Glycosylation of Renal and Hepatic γ-Glutamyl Transpeptidase from Normal Human Tissue[S]

• Published in: The Journal of biological chemistry Vol. 285; no. 38; pp. 29511 - 29524
• Main Authors: West, Matthew B., Segu, Zaneer M., Feasley, Christa L., Kang, Pilsoo, Klouckova, Iveta, Li, Chenglong, Novotny, Milos V., West, Christopher M., Mechref, Yehia, Hanigan, Marie H.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 17.09.2010; American Society for Biochemistry and Molecular Biology
• Subjects: Aged; Amino Acid Sequence; Blotting, Western; Electrophoresis, Polyacrylamide Gel; Female; gamma-Glutamyltransferase - chemistry; gamma-Glutamyltransferase - metabolism; gamma-Glutamyltranspeptidase; Genomics and Proteomics; GGT; Glycobiology and Extracellular Matrices; Glycopeptides; Glycoprotein; Glycosylation; Humans; In Vitro Techniques; Kidney; Kidney - enzymology; Liver; Liver - enzymology; Middle Aged; Molecular Sequence Data; Post-translational Modification; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Tandem Mass Spectrometry; gamma-Glutamyltranspeptidase; Post-translational Modification; GGT; Liver; Glycoprotein; Glycosylation; Glycopeptides; Kidney

The cell surface glycoprotein γ-glutamyl transpeptidase (GGT) was isolated from healthy human kidney and liver to characterize its glycosylation in normal human tissue in vivo. GGT is expressed by a single cell type in the kidney. The spectrum of N-glycans released from kidney GGT constituted a subs...