Clinical Chemistry, Vol 30, 1965-1971, Copyright © 1984 by American Association for Clinical Chemistry

Identification of coordinate pairs of polypeptides: a technique for screening of putative precursor product pairs in 2D gels

PF Lemkin, P Sonderegger and LE Lipkin

Two-dimensional electrophoresis, combined with computerized quantification of individual proteins, provides a sensitive and accurate approach to detection of small differences in the protein pattern. As an extension of "GELLAB," a data base system for the analysis of two-dimensional electrophoretic gels, we report here on a screening algorithm for detection of certain post-translational modification events. It is based on the assumption that, if there is a post-translational modification of a protein in the transition between two functional states of a biological system, in many cases the sum of the protein concentration of a precursor-product pair in one is equivalent to that in the other. In addition to the identification of candidate pairs with a precursor-product relationship, cues to the nature of the post-translational modification that might relate them might also be derived from comparisons of the isoelectric point and apparent molecular mass. This subset of the GELLAB system may be thought of as a screening tool in the search for and investigation of post-translational protein-processing events so that the more time- consuming structural investigations to follow can be performed on a smaller set of proteins.