Chemical Cleavage of Human Phosphoglucose Isomerase at Cysteine
Description:
The present study has resulted in the development of a procedure for the specific chemical fragmentation of human phosphoglucose isomerase into a minimal number of peptides. A two-cycle procedure for cleaving the protein with 2-nitro-5- thiocyanobenzoic acid results in four primary peptides and three overlap peptides. The peptides can be readily separated on the basis of their size by using sodium dodecyl sulfate polyacrylamide gel electrophoresis. Preliminary peptide alignments have been consi…
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Date:
December 1975
Creator:
Conn, Worth R.