Biotinylated peptides/proteins. II. Identification of biotinylated lysyl phenylthiohydantoins

John S. Smith; Brian T. Miller; Alexander Kurosky

doi:10.1016/0003-2697(91)90385-7

Biotinylated peptides/proteins. II. Identification of biotinylated lysyl phenylthiohydantoins

John S. Smith, Brian T. Miller, Alexander Kurosky

Neurobiology

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

The identification and characterization of biotinylated lysyl residues in a polypeptide chain by automated sequence analysis is described. An in depth analytical study was conducted for the delineation of Nε{lunate} modification of lysyl residues with N-hydroxysuccinimide esters of biotin and 6-aminohexanoic biotin. Confirmation of the structure of the phenylthiohydantoin derivatives of Nε{lunate} biotinylated lysine was achieved by mass spectrometry. The analytical study focused on the identification of biotinylated lysine-4 of neuropeptide Y which served as a model peptide for the analytical procedures detailed.

Original language	English (US)
Pages (from-to)	254-257
Number of pages	4
Journal	Analytical Biochemistry
Volume	197
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(91)90385-7
State	Published - Aug 15 1991

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0003-2697(91)90385-7

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title = "Biotinylated peptides/proteins. II. Identification of biotinylated lysyl phenylthiohydantoins",

abstract = "The identification and characterization of biotinylated lysyl residues in a polypeptide chain by automated sequence analysis is described. An in depth analytical study was conducted for the delineation of Nε{lunate} modification of lysyl residues with N-hydroxysuccinimide esters of biotin and 6-aminohexanoic biotin. Confirmation of the structure of the phenylthiohydantoin derivatives of Nε{lunate} biotinylated lysine was achieved by mass spectrometry. The analytical study focused on the identification of biotinylated lysine-4 of neuropeptide Y which served as a model peptide for the analytical procedures detailed.",

author = "Smith, {John S.} and Miller, {Brian T.} and Alexander Kurosky",

note = "Funding Information: i This work was supported by the National Institutes of Health Grant NS 29261 (to A.K.), Grant H-1190 from the Robert A. Welch Foundation (to A.K.), and National Institutes of Health Grant RR00317 (to K. Biemann).",

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doi = "10.1016/0003-2697(91)90385-7",

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T1 - Biotinylated peptides/proteins. II. Identification of biotinylated lysyl phenylthiohydantoins

AU - Smith, John S.

AU - Miller, Brian T.

AU - Kurosky, Alexander

N1 - Funding Information: i This work was supported by the National Institutes of Health Grant NS 29261 (to A.K.), Grant H-1190 from the Robert A. Welch Foundation (to A.K.), and National Institutes of Health Grant RR00317 (to K. Biemann).

PY - 1991/8/15

Y1 - 1991/8/15

N2 - The identification and characterization of biotinylated lysyl residues in a polypeptide chain by automated sequence analysis is described. An in depth analytical study was conducted for the delineation of Nε{lunate} modification of lysyl residues with N-hydroxysuccinimide esters of biotin and 6-aminohexanoic biotin. Confirmation of the structure of the phenylthiohydantoin derivatives of Nε{lunate} biotinylated lysine was achieved by mass spectrometry. The analytical study focused on the identification of biotinylated lysine-4 of neuropeptide Y which served as a model peptide for the analytical procedures detailed.

AB - The identification and characterization of biotinylated lysyl residues in a polypeptide chain by automated sequence analysis is described. An in depth analytical study was conducted for the delineation of Nε{lunate} modification of lysyl residues with N-hydroxysuccinimide esters of biotin and 6-aminohexanoic biotin. Confirmation of the structure of the phenylthiohydantoin derivatives of Nε{lunate} biotinylated lysine was achieved by mass spectrometry. The analytical study focused on the identification of biotinylated lysine-4 of neuropeptide Y which served as a model peptide for the analytical procedures detailed.

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Biotinylated peptides/proteins. II. Identification of biotinylated lysyl phenylthiohydantoins

Abstract

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