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J. Biol. Chem., Vol. 255, Issue 20, 9769-9772, 10, 1980
JD Termine, AB Belcourt, MS Miyamoto and KM Conn
After an initial 4 M guanidine HCl extraction to remove enamel
contaminants, subsequent guanidine HCl/EDTA extraction of fetal bovine
molar dentin removes almost all of the high molecular weight phosphoprotein
from the tissue in a single step. The fetal bovine dentin phosphoprotein is
then purified by a series of ion exchange (DEAE-cellulose or
DEAE-Se-phacel) and gel filtration (Sepharose CL-6B) chromatographic steps,
all under denaturing elution conditions in 7 M urea (ion exchange) or 4 M
guanidine HCl (gel filtration). The final purified phosphoprotein product
was chromatographically and electrophoretically homogenous. The apparent
molecular weight for this fetal bovine dentin phosphoprotein was
approximately 100,000 both by 4 M guanidine HCl gel filtration and
polyacrylamide gel electrophoresis in the presence of sodium dodecyl
sulfate. This value is considerably higher than those previously reported
for any other dentin phosphoprotein preparation. Roughly half of the total
serine residues in the protein were phosphorylated and these residues
together with aspartic acid comprised approximately 80% of the total
polypeptide backbone. The purified fetal bovine dentin phosphoprotein was
also glycosylated, containing approximately 6 galactosamine, 2 to 3
glucosamine, and 2 to 3 sialic acid residues/mol.
Properties of dissociatively extracted fetal tooth matrix proteins. II. Separation and purification of fetal bovine dentin phosphoprotein
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