Chemical Cleavage of Human Phosphoglucose Isomerase at Cysteine Page: 2
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The wide range of biochemical effects which result from
these genetic modifications of human PGI make this an ideal
system for basic structural-functional studies on this
enzyme. Though the variant forms of PGI are found in only
a small per cent of the human population, they are easily
recognized by clinical screening programs utilizing elec-
trophoretic methods. The unique electrophoretic mobilities
of these genetic variants are usually responsible for their
identification and ultimately will permit the elucidation of
the molecular basis of mutations.
The protocol for such an investigation is deceptively
simple. Fragmentation of the variant enzymes is followed
by comparison of the electrophoretic properties of the resul-
tant peptides with corresponding peptides from wild type PGI.
Further fragmentation of the nonidentical peptides should
eventually permit identification of amino acid changes which
result from the mutation.
Studies of PGI from human sources have been greatly
facilitated by an excellent isolation procedure developed
by Gracy and Tilley (11). Slight modification of the pro-
cedure allowed the isolation of homogeneous PGI in high yield
from erythrocytes, as well as from other tissues. The pro-
cedure is based upon a specific ligand-induced elution of
the enzyme from a phosphocellulose column utilizing either of
the substrates, fructose-6-phosphate or glucose-6-phosphate.
A 30,000 fold purification with 65 - 70% overall recovery
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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/m1/4/: accessed November 16, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .