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Investigation of sulfhydryl groups in cabbage phospholipase D by combination of derivatization methods and matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry
Author(s) -
Hwang InSeong,
Park SungJun,
Roh Taeyoung,
Choi MyungUn,
Kim HieJoon
Publication year - 2001
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(20010130)15:2<110::aid-rcm200>3.0.co;2-r
Subject(s) - chemistry , iodoacetic acid , chromatography , mass spectrometry , derivatization , matrix assisted laser desorption/ionization , cysteine , reagent , desorption , matrix (chemical analysis) , protein mass spectrometry , tandem mass spectrometry , biochemistry , organic chemistry , enzyme , adsorption
Abstract All eight cysteine residues in 92 kDa cabbage phospholipase D (PLD), deduced from the cDNA sequence, were shown to have free sulfhydryl groups by analysis using matrix‐assisted laser desorption/ionization time‐of‐flight mass spectrometry (MALDI‐TOFMS) of tryptic peptides of PLD derivatized with p ‐chloromercurybenzoate, iodoacetic acid, and N ‐ethylmaleimide, as well as of underivatized PLD. Assignment of sulfhydryl groups by any one method was not conclusive. However, complementary information derived from tryptic peptides derivatized with different reagents made full assignment of sulfhydryl groups possible. Copyright © 2001 John Wiley & Sons, Ltd.