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 |
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| container_title | Molecular immunology |
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| creator | GREBENAU, R. C GOLDENBERG, D. M CHIEN-HSING CHANG KOCH, G. A GOLD, D. V KUNZ, A HANSEN, H. J |
| description | 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 IMMU-MN3 antibody. Based on Concanavalin A affinity chromatography, enzymatic digestion with Endoglycosidase F and carbohydrate analysis, it was found that the heterogeneity detected by SDS-PAGE and HIC was due to differences in glycosylation. Furthermore, sequential gel analysis (non-reduced/reduced) demonstrated that the upper heavy-chain band was asymmetrically glycosylated. |
| doi_str_mv | 10.1016/0161-5890(92)90185-Z |
| format | Article |
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Furthermore, sequential gel analysis (non-reduced/reduced) demonstrated that the upper heavy-chain band was asymmetrically glycosylated.</description><identifier>ISSN: 0161-5890</identifier><identifier>EISSN: 1872-9142</identifier><identifier>DOI: 10.1016/0161-5890(92)90185-Z</identifier><identifier>PMID: 1603094</identifier><identifier>CODEN: MOIMD5</identifier><language>eng</language><publisher>Oxford: Elsevier</publisher><subject>Animals ; Antibodies, immunoglobulins ; Antibodies, Monoclonal - chemistry ; Biological and medical sciences ; Blotting, Western ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. 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Furthermore, sequential gel analysis (non-reduced/reduced) demonstrated that the upper heavy-chain band was asymmetrically glycosylated.</description><subject>Animals</subject><subject>Antibodies, immunoglobulins</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Glycosylation</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin Heavy Chains - chemistry</subject><subject>In Vitro Techniques</subject><subject>Macromolecular Substances</subject><subject>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - pharmacology</subject><subject>Mice</subject><subject>Molecular immunology</subject><subject>Structure</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkD1PwzAQhi0EKqXwD0DygBAMATuOk3gsFS2Vilhg6WI59rkY5aPYyZB_T0qrMpxuuOc93T0IXVPySAlNn4aiEc8FuRfxgyA059H6BI1pnsWRoEl8isZH5BxdhPBNCElJykdoRFPCiEjGaPnmtG--oAXfbKAG1_a4sVjhbeeddWDwcrOg2HSA2war0FcVtN5pPJ8-403Z6yb0pWpdU1-iM6vKAFeHPkGf85eP2Wu0el8sZ9NVpBmjbcSMzpUV3DKec1pkJosp5EJlw0kkzTKmUgM6LxKuSEGMAQCd2ZQRpkRhDGcTdLffu_XNTwehlZULGspS1dB0QWaMDC5EPIDJHhweDMGDlVvvKuV7SYncGZQ7PXKnR4pY_hmU6yF2c9jfFRWY_9Be2TC_PcxV0Kq0XtXahSPGGRfJgP4Ccid4pA</recordid><startdate>19920601</startdate><enddate>19920601</enddate><creator>GREBENAU, R. 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Psychology</topic><topic>Fundamental immunology</topic><topic>Glycosylation</topic><topic>Immunoglobulin Fab Fragments - chemistry</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin Heavy Chains - chemistry</topic><topic>In Vitro Techniques</topic><topic>Macromolecular Substances</topic><topic>Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase - pharmacology</topic><topic>Mice</topic><topic>Molecular immunology</topic><topic>Structure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>GREBENAU, R. C</creatorcontrib><creatorcontrib>GOLDENBERG, D. M</creatorcontrib><creatorcontrib>CHIEN-HSING CHANG</creatorcontrib><creatorcontrib>KOCH, G. A</creatorcontrib><creatorcontrib>GOLD, D. V</creatorcontrib><creatorcontrib>KUNZ, A</creatorcontrib><creatorcontrib>HANSEN, H. 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| fulltext | fulltext |
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| ispartof | Molecular immunology, 1992-06, Vol.29 (6), p.751-758 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 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 |
| title | Microheterogeneity of a purified IgG1 due to asymmetric FAB glycosylation |
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