Chemical Cleavage of Human Phosphoglucose Isomerase at Cysteine Page: 2
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Conn, Worth R., Chemical Cleavage" of Human Phosphoglu-
cose Isomerase'at Cysteine. Master of Science (Chemistry),
December, 1975, 69 pp., 3 tables, bibliography, 33 titles.
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 spe-
cific genetic mutations of human phosphoglucose isomerase.
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Conn, Worth R. Chemical Cleavage of Human Phosphoglucose Isomerase at Cysteine, thesis, December 1975; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc663679/m1/2/: accessed January 21, 2019), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .