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Immobilization of Antibodies on Magnetic Carbonaceous Microspheres for Selective Enrichment of Lysine-acetylated Proteins and Peptides

Lysine acetylation is a dynamic and reversible modification, which has been proved to be a key posttransla- tional modification in cellular regulation. However, the low amounts of the acetylated proteins could hardly be de- tected before enrichment. In this study, for the first time, antibody-immobi...

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Bibliographic Details
Published in:Chinese journal of chemistry 2012-10, Vol.30 (10), p.2549-2555
Main Author: 王莹寅 姚望 杨芃原 邓春晖 樊惠芝
Format: Article
Language:English
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Summary:Lysine acetylation is a dynamic and reversible modification, which has been proved to be a key posttransla- tional modification in cellular regulation. However, the low amounts of the acetylated proteins could hardly be de- tected before enrichment. In this study, for the first time, antibody-immobilized magnetic carbonaceous micro- spheres were developed for selective enrichment of acetylated proteins and peptides. At first, standard proteins composed of acetylated bovine serum albumin, myoglobin, a-casein and ovalbumin were used as model proteins to verify the enrichment efficiency. Then, the synthesized peptide was employed to confirm the selectivity of the method. Besides, the antibody-immobilized magnetic particles were successfully applied to analyze mouse mito- chondrial proteins. After database search, 29 acetylated sites in 26 proteins were identified.
ISSN:1001-604X
1614-7065
DOI:10.1002/cjoc.201200542