Reversible covalent binding of the fluorophore epicocconone to proteins provides a novel approach to the sensitive quantification of proteins across a wide variety of different platforms

D. Veal; J. Mackintosh; D. Coghlan; Y. Choi; P. Karuso

Reversible covalent binding of the fluorophore epicocconone to proteins provides a novel approach to the sensitive quantification of proteins across a wide variety of different platforms

D. Veal, J. Mackintosh, D. Coghlan, Y. Choi, P. Karuso

Research output: Contribution to journal › Meeting abstract › peer-review

Original language	English
Pages (from-to)	S380-S380
Number of pages	1
Journal	Molecular and Cellular Proteomics
Volume	4
Issue number	8S1
Publication status	Published - Aug 2005
Event	HUPO (Human Proteome Organisation) 4th Annual World Congress - Munich, Germany Duration: 29 Aug 2005 → 1 Sept 2005

Access to Document

http://www.mcponline.org/content/4/8_suppl_1#Information

Cite this

@article{58ca5f7358974fd78c542e43f389c93b,

title = "Reversible covalent binding of the fluorophore epicocconone to proteins provides a novel approach to the sensitive quantification of proteins across a wide variety of different platforms",

author = "D. Veal and J. Mackintosh and D. Coghlan and Y. Choi and P. Karuso",

year = "2005",

month = aug,

language = "English",

volume = "4",

pages = "S380--S380",

journal = "Molecular and Cellular Proteomics",

issn = "1535-9476",

publisher = "American Society for Biochemistry and Molecular Biology",

number = "8S1",

note = "HUPO (Human Proteome Organisation) 4th Annual World Congress ; Conference date: 29-08-2005 Through 01-09-2005",

}

Veal, D, Mackintosh, J, Coghlan, D, Choi, Y & Karuso, P 2005, 'Reversible covalent binding of the fluorophore epicocconone to proteins provides a novel approach to the sensitive quantification of proteins across a wide variety of different platforms', Molecular and Cellular Proteomics, vol. 4, no. 8S1, pp. S380-S380. <http://www.mcponline.org/content/4/8_suppl_1#Information>

Reversible covalent binding of the fluorophore epicocconone to proteins provides a novel approach to the sensitive quantification of proteins across a wide variety of different platforms. / Veal, D.; Mackintosh, J.; Coghlan, D. et al.
In: Molecular and Cellular Proteomics, Vol. 4, No. 8S1, 08.2005, p. S380-S380.

Research output: Contribution to journal › Meeting abstract › peer-review

TY - JOUR

T1 - Reversible covalent binding of the fluorophore epicocconone to proteins provides a novel approach to the sensitive quantification of proteins across a wide variety of different platforms

AU - Veal, D.

AU - Mackintosh, J.

AU - Coghlan, D.

AU - Choi, Y.

AU - Karuso, P.

PY - 2005/8

Y1 - 2005/8

M3 - Meeting abstract

SN - 1535-9476

VL - 4

SP - S380-S380

JO - Molecular and Cellular Proteomics

JF - Molecular and Cellular Proteomics

IS - 8S1

T2 - HUPO (Human Proteome Organisation) 4th Annual World Congress

Y2 - 29 August 2005 through 1 September 2005

ER -