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Anal Biochem

Title:		Mass spectrometric signature of S-prenylated cysteine peptides
Author(s):		Tuinman AA; Thomas DA; Cook KD; Xue CB; Naider F; Becker JM;
Address:		"Department of Chemistry, University of Tennessee, Knoxville 37996"
Journal Title:		Anal Biochem
Year:		1991
Volume:		193
Issue:		2
Page Number:		173 - 177
DOI:		10.1016/0003-2697(91)90004-d
ISSN/ISBN:		0003-2697 (Print) 0003-2697 (Linking)
Abstract:		"The fast atom bombardment mass spectra of peptides containing S-prenylated cysteine display signature fragmentations characteristic of this modified amino acid. The fragmentation is independent of the nature of the cysteine carbonyl substituent, easily differentiates prenyl from nonprenyl alkylation, and readily identifies the oligomer count of the prenyl. This screening method, which requires little time, effort, or material (compared with previous analysis methods based on chemical degradation), greatly facilitates the identification of these prenylated proteins"
Keywords:		"Amino Acid Sequence Cysteine/*chemistry Mating Factor Molecular Sequence Data Oligopeptides/*chemistry Peptide Fragments/*chemistry Peptides/*chemistry Protein Processing, Post-Translational Spectrometry, Mass, Fast Atom Bombardment;"
Notes:		"MedlineTuinman, A A Thomas, D A Cook, K D Xue, C B Naider, F Becker, J M eng GM-22086/GM/NIGMS NIH HHS/ GM-22087/GM/NIGMS NIH HHS/ Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1991/03/02 Anal Biochem. 1991 Mar 2; 193(2):173-7. doi: 10.1016/0003-2697(91)90004-d"