Characterization of Human Glucose-6-Phosphate Isomerase of Different Sizes Page: 2
vii, 80 leaves: ill.View a full description of this thesis.
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Sun, An Qiang, CHARACTERIZATION OF HUMAN GLUCOSE-6-
PHOSPHATE ISOMERASE ISOZYMES OF DIFFERENT SIZES. Master of
Science (Biochemistry) , December, 1989, 80 pp., 5 tables, 13
illustrations, bibliography, 112 titles.
Glucose phosphate isomerase (GPI) was purified from
human placenta utilizing cross-linked spherical particle
phosphocellulose. In three steps, GPI could be purified
approximately 5500 fold with greater than 50% recovery. The
purified enzyme exhibited four bands upon non-denaturing PAGE
and isoelectric focusing (IEF) when stained with GPI specific
activity stain. The four isozymes were isolated by
preparative IEF. The isoelectric points of the isozymes were
determined. Sodium dodecyl sulfate (SDS) gel electrophoresis
showed two types of subunits with different molecular
weights. Structural analyses showed both types of subunits
had blocked amino termini. Other properties of the isozymes
and subunits, including immunological reactivity, pH
stability, peptide mapping and amino acid composition, were
also established.:
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Sun, An Qiang. Characterization of Human Glucose-6-Phosphate Isomerase of Different Sizes, thesis, December 1989; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc500752/m1/2/: accessed July 17, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .