RE: MALDI-TOF Ion supression

Amina S. Woods (awoods@jhmi.edu)
Mon, 06 Dec 1999 15:36:35 -0500

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Brett:
I don't know of a good reference, but basically suppression is usually
linked to the various peptides amino acid composition. Those peptides that
can be easily protonated (the ones that have one or more arg or lys are the
ones that desorb best. If you buffer your sample solution,thus increasing
the pH of the sample matrix mixture from <2 to >4, you will get those
peptides that have less basic residue to desorb. I showed that in a paper,
I'll give you the reference.

A.S. Woods, A.Y.C. Huang, R.J. Cotter, G.R. Pasternack, D.M. Pardoll and
E.M. Jaffee. Simplified High Sensitivity Sequencing of MHC Class
I-Associated, Immunoreactive Peptides Using Matrix Assisted Laser
Desorption/Ionization Mass Spectrometry, Anal. Biochem. 226 (1995) 15-25.

Hope it helps.

Amina

Amina S. Woods, Ph.D.
NIDA Intramural Program, NIH
5500 Nathan Schock Drive
Baltimore, MD 21224
Tel: 410-550-1507
Fax: 410-550-2971
e-mail: awoods@intra.nida.nih.gov
-----Original Message-----
From: Association of Biomolecular Resource Facilities
[mailto:abrf-request@aecom.yu.edu]On Behalf Of Brett Phinney
Sent: Monday, December 06, 1999 12:15 PM
To: Recipients of ABRF List
Subject: MALDI-TOF Ion supression

I am trying to find a good reference that explains and documents the ion
suppression phenomena seen when analyzing complex mixtures such as peptides
by MALDI. Does anyone know of such a reference?

Thanks a lot

Brett Phinney
Department of Biochemistry
North Carolina State University

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Brett:
    I don't know of a good = reference,=20 but basically suppression is usually linked to the various peptides = amino acid=20 composition.  Those peptides that can be easily protonated (the = ones that=20 have one or more arg or lys are the ones that desorb best.  If = you=20 buffer your sample solution,thus increasing the pH of the sample matrix = mixture=20 from <2 to >4, you will get those peptides that have less basic = residue to=20 desorb. I showed that in a paper, I'll give you the=20 reference.
 

A.S. = Woods, A.Y.C. Huang,=20 R.J. Cotter, G.R. Pasternack, D.M. Pardoll and E.M. Jaffee. Simplified = High=20 Sensitivity Sequencing of MHC Class I-Associated, Immunoreactive = Peptides Using=20 Matrix Assisted Laser Desorption/Ionization Mass Spectrometry, Anal. = Biochem.=20 226 (1995) 15-25.

Hope it helps.

Amina

Amina S. Woods, Ph.D.
NIDA Intramural Program, NIH
5500 Nathan Schock Drive
Baltimore, MD 21224
Tel: 410-550-1507
Fax: 410-550-2971
e-mail: awoods@intra.nida.nih.gov
-----Original Message-----
From: Association of = Biomolecular=20 Resource Facilities [mailto:abrf-request@aecom.yu.edu]On Behalf Of=20 Brett Phinney
Sent: Monday, December 06, 1999 12:15=20 PM
To: Recipients of ABRF List
Subject: MALDI-TOF = Ion=20 supression

I am trying to find a good reference that explains = and=20 documents the ion suppression phenomena seen when analyzing complex = mixtures=20 such as peptides by MALDI. Does anyone know of such a = reference?
 
 
Thanks a lot
 
 
Brett Phinney
Department of Biochemistry
North Carolina State University
 
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