Wei -
As an alternative to citraconic anhydride, you might consider
3,4,5,6-tetrahydrophthaloyl anhydride; see Gibbons and Schachman,
Biochemistry 15 (1976) 52. Reaction with lysine residues is reversible, as
with citraconic anhydride. Unlike citraconic anhydride, it can be removed
with mild conditions (pH < 6).
Andy Alpert
PolyLC Inc.
(410) 992-5400
***********************************************
<< Subj: Re: lysine specific protease
Date: 09/12/2000 8:35:22 PM Eastern Daylight Time
From: fperini@unmc.edu
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I was successful by using acetylation.This was done on a peptide whose
N-terminal sequence was known,and it
allowed me to complete the sequence of a protein.See:E J.M. Van Damme,et
al.,Eur.J.Biochem,vol.202,23-30(1991) on
sequence of snowdrop lectin.I am not familiar with the chemical that you
suggest.I also used citraconic anhydride to
block lysine epsilon amino group reversibly,but it is tricky.
To: Recipients of ABRF List <abrf@aecom.yu.edu>
Subject: lysine specific protease
Hi Folks,
I'm looking for a protease that is specific to lysine. I've read in a
paper about A. mellea protease that can be one. I don't know if it's
commercially available or if there are other ones that can do it.
I am also looking for possible reagents that can block lysine residues,
like ethyl thiotrifluoroacetate. Any information on that will be very
appreciated.
Many, many thanks!
Wei Wu
Department of Chemistry
Michigan State University
East Lansing, MI 48824
1-517-353-6767
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