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DISCONTINUOUS ELECTROPHORESIS OF PEPSIN AND PEPSINOGEN IN THIN SHEETS OF POLYACRYLAMIDE GEL

LEW CUNNINGHAM 1, ELLEN M. RASCH 1, ANN L. LEWIS 1, and RICHARD HEITSCH 1

1 Department of Anatomy, Marquette School of Medicine, and Department of Biology, Marquette University, Milwaukee, Wisconsin 53233

Electrophoretic separation of discrete protein bands from solutions of crystalline pepsin or pepsinogen was accomplished in a system incorporating pH discontinuity and using standard, glass microslides to support thin (0.25-mm) sheets of 15% polyacrylamide gel. Adherence of gel films to a glass support during fixation and staining with crystal violet not only prevented distortion of gels as a result of swelling, but also provided preparations that could be readily scanned with a microspectrophotometer. A number of discrete peptide bands were identified from different samples of purified pepsin. Among the several heterogeneous components found in commercially available samples of crystalline pepsinogen, there was a characteristic impurity, the mobility of which was directly comparable to that of pepsin run under the same conditions of electrophoresis. Specific details of methodology are presented.

Submitted on June 24, 1970


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