Abstract
Described here is a method used to determine the sialic acid content of the structurally distinct carbohydrates attached at N77 and N101 of bovine prothrombin fragment 1. The protein is proteolytically cleaved with a α-chymotrypsin to release two glycopeptides, each containing one of the two glycosylation sites. Electrospray ionization mass spectrometry and capillary electrophoresis are used to determine the structural difference between the carbohydrates of each of these glycopeptides. N77 bears a carbohydrate containing as many as 4 sialic acid (N-acetylneuraminic acid) residues, whereas the carbohydrate attached at N101 may carry as many as 5 sialic acid residues. Partially desialated forms of both of the native carbohydrate chains are observed. For both the N77 and N101-linked carbohydrates, the 1. 2, and 3-sialic acid-containing forms predominate. UV absorbance detection of the peptide-free, underivatized carbohydrate moieties is also demonstrated.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Journal of Liquid Chromatography & Related Technologies
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
