|
|||||
|
|
Human non-secretory ribonucleases. II. Structural characterization of theN-glycans of the kidney, liver and spleen enzymes by NMR spectroscopy and electrospray mass spectrometry |
|
| Authors: | Lawrence Cris W; Little Pamela A; Little Brian W; Glushka John; van Halbeek Herman; Alhadeff Jack A |
| Institution: | 1Department of Chemistry, Division of Biochemical Sciences, Lehigh University Bethlehem, PA 18015 2Neuropathology Laboratory, Lehigh Valley Hospital 1200 South Cedar Crest Boulevard, Allentown, PA 18105 3Complex Carbohydrate Research Center and Department of Biochemistry, University of Georgia Athens, GA 30602-4712, USA |
| Abstract: | The N-glylycans have been removed by peptide-N-glycosidase F(PNGase F) from purified human non-secretory RNases derivedfrom kidney, liver and spleen. The spleen RNase was purifiedby two procedures, one of which did not include the usual acidtreatment step (0.25 M H2SO4, 45 min, 4C), to determine ifacid treatment alters the carbohydrate moieties. TheN-glycansof the RNases were fractionated by Bio-Gel P-4 chromatographyand analysed by 600 MHz 1H-NMR spectroscopy and electrospraymass spectrometry. All four non-secretory RNase preparationscontained the following structures: The relative amounts of the trisaccharide, pentasaccharide andhexasaccharide appeared to vary slightly in the different tissueRNases. The overall results indicate: (i) that acid treatmentduring purification does not alter the N-glycans of non-secretoryRNases; (ii) that the N-glycans from kidney, liver and spleennon-secretory RNases are very similar, if not identical, toone another, but different from the N-glycan structures reportedfor secretory RNase. N-glycans non-secretory RNases |
| Keywords: | |
| 本文献已被 Oxford 等数据库收录！ | |