Analysis of N‐acetyl‐4‐O‐acetylneuraminic‐acid‐containing. N‐linked carbohydrate chains released by peptide‐N4‐(N‐acetyl‐β‐glucosaminyl)asparagine amidase F
- 3 March 1989
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 180 (1) , 101-110
- https://doi.org/10.1111/j.1432-1033.1989.tb14620.x
Abstract
The carbohydrate chains of equine fibrinogen were enzymatically released by peptide-N4-(N-acetyl-.beta.-glucosaminyl)asparagine amidase F. The oligosaccharides obtained were fractionated by a combination of FPLC and HPLC and analyzed by 500-MHz 1H-NMR spectroscopy. Four monosialo and four disialo diantennary N-acetyllactosamine type of carbohydrate chains occur.This publication has 26 references indexed in Scilit:
- A general strategy for the isolation of carbohydrate chains fromN-,O-glycoproteins and its application to human chorionic gonadotrophinGlycoconjugate Journal, 1987
- Migration of O‐acetyl groups in N,O‐acetylneuraminic acidsEuropean Journal of Biochemistry, 1987
- Primary structure of two major glycans of bovine fibrinogenEuropean Journal of Biochemistry, 1985
- FIBRINOGEN AND FIBRINAnnual Review of Biochemistry, 1984
- Structure, biosynthesis and functions of glycoprotein glycansCellular and Molecular Life Sciences, 1982
- High‐Resolution 1H‐NMR Spectroscopy of Free and Glycosidically Linked O‐ Acetylated Sialic AcidsEuropean Journal of Biochemistry, 1982
- An autosomal dominant gene regulates the extent of 9-O-acetylation of murine erythrocyte sialic acids. A probable explanation for the variation in capacity to activate the human alternate complement pathway.The Journal of Experimental Medicine, 1980
- The amino acid sequence of a 27-residue peptide feleased from the α-chain carboxy-terminus during the plasmic digestion of human fibrinogenBiochemical and Biophysical Research Communications, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970