Microheterogeneity of a purified IgG1 due to asymmetric FAB glycosylation

A murine monoclonal anti-granulocyte IgG1, IMMU-MN3, was seen to exhibit heterogeneity. On reduced SDS-PAGE, the purified antibody appeared as two heavy-chain bands of unequal intensity, and only one light-chain band. Hydrophobic interaction chromatography (HIC) also resolved two populations of the...

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Veröffentlicht in:	Molecular immunology 1992-06, Vol.29 (6), p.751-758
Hauptverfasser:	GREBENAU, R. C, GOLDENBERG, D. M, CHIEN-HSING CHANG, KOCH, G. A, GOLD, D. V, KUNZ, A, HANSEN, H. J
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antibodies, immunoglobulins Antibodies, Monoclonal - chemistry Biological and medical sciences Blotting, Western Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Fundamental immunology Glycosylation Immunoglobulin Fab Fragments - chemistry Immunoglobulin G - chemistry Immunoglobulin Heavy Chains - chemistry In Vitro Techniques Macromolecular Substances Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - pharmacology Mice Molecular immunology Structure
Online-Zugang:	Volltext
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