Infrared spectroscopy used to evaluate glycosylation of proteins.
Infrared (IR) spectroscopy is used for studying the carbohydrate moieties of glycosylated proteins. IR spectra of mono- and disaccharides in the fingerprint region are specific to each sugar and to the environment of the sugar molecules (i.e., aqueous solution or anhydrous glass phase). The IR spectra of glycosylated proteins (mucin, soybean peroxidase, collagen IV, and avidin) were compared with those of the constituent sugars and cytochrome c (a protein with no glycosylation). Our results demonstrate that the IR absorption spectra of glycosylated proteins show distinct absorption bands for the sugar moiety, the protein amide group, and water. Therefore, IR can be used to detect glycosylation.
Khajehpour
Mazdak
M
Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Dashnau
Jennifer L
JL
Vanderkooi
Jane M
JM
D000042:Absorption; D001360:Avidin / Q000737:chemistry; D002241:Carbohydrates / Q000737:chemistry; D024141:Collagen Type IV / Q000737:chemistry; D006031:Glycosylation; D008958:Models, Molecular; D009077:Mucins / Q000737:chemistry; D010544:Peroxidases / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012680:Sensitivity and Specificity; D013025:Glycine max / Q000737:chemistry; D013055:Spectrophotometry, Infrared
D002241:Carbohydrates; D024141:Collagen Type IV; D009077:Mucins; D011506:Proteins; D001360:Avidin; D010544:Peroxidases