Isolation and Characterization of Glycoproteins from 110 Day Old Ovine Fetal Diaphysial and Metaphysial Bone Fragments
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Authors
Allswede, Michael P.
Issue Date
1983
Type
Thesis
Language
en_US
Keywords
Alternative Title
Abstract
Glycoproteins, isolated from 110 day old fetal sheep
compact and spongy bone samples, were fractionated and
pooled according to order of elution from a molecular
exclusion chromatography column. The major pool in the case
of spongy and compact bone was investigated as to its
homogeneity, amino acid composition, hexosamine composition,
hexuronic acid composition, sialic acid composition, and
neutral sugar composition. Techniques utilized to
characterize the glycoproteins were molecular exclusion
chromatography, colorimetric hexosamine assay, resorcinol assay, and gas chromatography.
Glycoproteins isolated in this preparation were found to be
of heterogeneous molecular weights and sizes. The
glycoprotein fractions were, however, able to be pooled in
5-8 discreet pools based on similar protein, hexose, and
hexuronic acid composition. The major pools of the compact
and spongy bone samples were subjected to electrophoretic
analysis to ascertain homogeneity, in those instances, 5-7
definable bands were seen to correspond between the two
qlycoprotein preparations. The two major components (based
on dye intensity) were also seen to correspond with one
another. Further experimentation on the major oools of the
two bone preparations was done to rouqhly characterize the
glycoproteins in the pools and to aid in the further
separation of these molecules. It was found that the
protein in the molecules was composed of predominately
serine, threonine, glycine, and alanine residues with a
dearth of aromatic residues. The glycoproteins contained
small amounts of sialic acid, hexosamine, and hexuronic
acid. Larger amounts of hexose were found with galactose
and mannose the predominate neutral sugars. Further
separation is needed to accurately define the glycoproteins
present in this preparation.
Description
iv, 26 p.
Citation
Publisher
Kalamazoo College
License
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