JBC Focus on PI3-Kinase with Echelon

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Subtilisin BPN'

V. ISOLATION AND SEQUENCE OF CHYMOTRYPTIC PEPTIDES

Francis S. Markland 1, Gertrude Kreil 1, Bruno Ribadeau-Dumas 1, and Emil L. Smith 1

From the 1 From the Department of Biological Chemistry, UCLA School of Medicine, University of California, Los Angeles, California 90024

The diisopropylphosphoryl-derivative of subtilisin BPN' was denatured and digested with chymotrypsin. The peptides were separated initially on Dowex 1-X2 or Dowex 50-X2 and further purified by various methods. A total of 36 pure peptides was isolated and the sequences were partially or fully determined. These peptides provided many useful overlaps of peptides previously isolated from the tryptic digest. In addition, new peptides were isolated as well as others which confirmed sequences established from the tryptic digest. The sequence of the first 104 residues from the amino terminus is given.

Submitted on April 28, 1966


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