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Reaction monitoring of succinylation of collagen with matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Kim SungHo,
Lee JeoungHwa,
Yun ShinYoung,
Yoo JongShin,
Jun ChulHo,
Chung KwanYong,
Suh Hwal
Publication year - 2000
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/1097-0231(20001130)14:22<2125::aid-rcm141>3.0.co;2-6
Subject(s) - chemistry , succinylation , mass spectrometry , desorption , matrix (chemical analysis) , ambient ionization , chromatography , matrix assisted laser desorption/ionization , ionization , analytical chemistry (journal) , chemical ionization , organic chemistry , ion , biochemistry , lysine , adsorption , amino acid
Succinylated collagen was synthesized by the reaction of collagen with succinic anhydride under basic conditions for one hour. Using the matrix‐assisted laser desorption/ionization time‐of‐flight (MALDI‐TOF) technique, the reaction products were directly identified without multi‐step separation processes. MALDI‐MS monitored the reaction more accurately than the conventional method of sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS‐PAGE). From the change in molecular mass during the reaction, it is observed that about 28 succinyl groups are attached to the collagen strand. Copyright © 2000 John Wiley & Sons, Ltd.