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Chemical Cleavage of Human Phosphoglucose Isomerase at Cysteine

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 considered, and amino acid analyses have been performed. End-terminal analyses of the enzyme revealed a carboxyl terminal sequence of Asp-Val-Gln and a blocked amino terminus. The cysteine cleavage procedure provides an excellent method for the identification and location of specific genetic mutations of human phosphoglucose isomerase.

Identiferoai:union.ndltd.org:unt.edu/info:ark/67531/metadc663679
Date12 1900
CreatorsConn, Worth R.
ContributorsGracy, Robert W., Russell, Benny, Jacobson, Myron
PublisherNorth Texas State University
Source SetsUniversity of North Texas
LanguageEnglish
Detected LanguageEnglish
TypeThesis or Dissertation
Format69 leaves: ill., Text
RightsPublic, Conn, Worth R., Copyright, Copyright is held by the author, unless otherwise noted. All rights

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