Human non-secretory ribonucleases. II. Structural characterization of the N-glycans of the kidney, liver and spleen enzymes by NMR spectroscopy and electrospray mass spectrometry.
Publication/Presentation Date
6-1-1993
Abstract
The N-glycans have been removed by peptide-N-glycosidase F (PNGase F) from purified human non-secretory RNases derived from kidney, liver and spleen. The spleen RNase was purified by two procedures, one of which did not include the usual acid treatment step (0.25 M H2SO4, 45 min, 4 degrees C), to determine if acid treatment alters the carbohydrate moieties. The N-glycans of the RNases were fractionated by Bio-Gel P-4 chromatography and analysed by 600 MHz 1H-NMR spectroscopy and electrospray mass spectrometry. All four non-secretory RNase preparations contained the following structures: [formula: see text] The relative amounts of the trisaccharide, pentasaccharide and hexasaccharide appeared to vary slightly in the different tissue RNases. The overall results indicate: (i) that acid treatment during purification does not alter the N-glycans of non-secretory RNases; (ii) that the N-glycans from kidney, liver and spleen non-secretory RNases are very similar, if not identical, to one another, but different from the N-glycan structures reported for secretory RNase.
Volume
3
Issue
3
First Page
249
Last Page
259
ISSN
0959-6658
Published In/Presented At
Lawrence, C. W., Little, P. A., Little, B. W., Glushka, J., van Halbeek, H., & Alhadeff, J. A. (1993). Human non-secretory ribonucleases. II. Structural characterization of the N-glycans of the kidney, liver and spleen enzymes by NMR spectroscopy and electrospray mass spectrometry. Glycobiology, 3(3), 249–259. https://doi.org/10.1093/glycob/3.3.249
Disciplines
Medicine and Health Sciences
PubMedID
8358150
Department(s)
Department of Pathology and Laboratory Medicine
Document Type
Article