Electrophoretic Determination of Glycoproteins in Human Gingiva

The purpose of this investigation was to study the composition of glycoprotein fractions which could be isolated from the interstitial matrix of human gingival tissue, and from human serum. This study is considered important to the periodontist because of the intimate relationship between periodontal disease and oral connective tissue. | Gingival tissue, obtained during the course of routine periodontal treatment,, was pooled according to age and sex. A glycoprotein fraction was isolated by a procedure which included saline extraction, acidification to pH4, and ammonium sulfate precipitation. Inasmuch as all of the tissue collected exhibited some degree of inflammation, human palatal tissue taken at autopsy was used for comparison. Autologous serum samples and serum from individuals with no clinical evidence of oral inflammation were fractionated as well. The glycoproteins were analyzed using a polyacrylamide gel electrophoretic technique employing an E.C. apparatus. The conditions included a 5% gel matrix, tris buffer pH 8.6, y 8.4 x 10~3 with respect to the salt, 5°C for 3 hours. The gels were stained with fresh Amido Black 10B solution. | The glycoprotein isolated from gingival tissue was differentiated from palatal tissue glycoprotein by the presence of a darkly staining component which migrated approximately 4.03 cm. from origin. Palatal tissue has a similiar component which stains less intensely. A possible sex difference can be observed with the gingival glycoprotein fraction. A distinct pair of bands which stain with what is arbitrarily called medium intensity migrates between 5.15 and 5.70 cm. from the origin. With male gingiva there is an analogous band or pair of relatively unseparated bands which migrate with a trailing edge somewhat faster than the slowest female component and a leading edge somewhat slower than the fastest female component. | The serum glycoprotein fraction can be readily differentiated from that of gingiva or palate, inasmuch as the albumin component migrates at a slower rate than the major component present in the tissue fraction. Thus, if the electrophoretic patterns of the three glycoprotein fractions are observed together, an observer with little practice can readily distinguish the source of the fraction using the criteria previously described.

Grantor dc:publisher

Creighton University

Year dc:date.issued

1976

Author dc:creator

• Westnick, George Michael

Advisor dc:contributor.advisor

• Fishkin, Arthur F.

Statement dc:rights

• A non-exclusive distribution right is granted to Creighton University and to ProQuest following the publishing model selected above.

Language dc:language.iso

en_US

Handle dc:identifier.uri

http://hdl.handle.net/10504/118422

OAI identifier oai:identifier

oai:cdr.creighton.edu:10504/118422