Usually free trypsin is used for protein digestion, followed by LC-MS identification. For complex sample, free trypsin digestion usually need at least several hours. Immobilized trypsin, trypsin immobilized on various solid supports, usually can carry out the protein digestion within several minutes due to evidently higher trypsin concentration. Interestingly, many publications mentioned there were some extent complementarity between immobilized trypsin and free trypsin digestion in terms of the proteins identified. Does anyone have some ideas to understand the complementarity? Thanks.
Thank you for your response for the question.
I am thinking why the complementarity exists. It should be very close. Recently we make it clear I think in our publication (J Chromatogr A. 2014 Apr 11;1337:40-7). Actually, the complementarity in terms of protein identifications can be ignored.
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