Dear Peter,
I had a very similar problem with unmodified trypsin from Sigma. The protein I
used to work on contained a sequence ...EEFKPKPRPFMPN... and after tryptic
digest and affinity chromatography I observed several peptides whose masses
could be assigned to trypsin-specific cleavages at the second and third basic
residue within the KPKPRP sequence. The software I was using (GPMAW) also does
by default not consider a tryptic cleavage N-terminal of Pro. I asked Peter
Hojrup from Odense university (who is the author of the programm) for some
literature for the cleavage resistance of X-Pro bonds. He gave me some
citations but not all of them mention this fact. E.g. in "Proteolytic enzymes"
by Beynon and Bond there is no mentioning of this resistance, while in G.
Allens "Sequencing of Proteins and Peptides" there is.
In my opinion, normally a cleavage before Pro will be more or less unlikely.
However in special cases such as special sterical conditions or anything else
it might occur in remarkable extent (in my case these had been the only signals
observed!).
So maybe your your supervisor had been correct for the usual cases while there
are some exceptions from this rule of thumb.
Yours sincerely,
Marcus
-- * Marcus Macht, AG Przybylski, Faculty of Chemistry, University of Konstanz * Box M 732, 78457 Konstanz, Germany * Tel:++49-7531-883391 / Fax:++49-7531-883097 * Email: macht@sgiclu.chemie.uni-konstanz.de * URL: http://www.ag-przybylski.chemie.uni-konstanz.de/~macht