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Characterization of Some Glycopeptides of Ovomucin.

AUREA MALABAG ALMAZAN, University of Nebraska - Lincoln

Abstract

In a number of studies reported in the literature, isolation of ovomucin by such methods as ammonium sulfate fractionation (1,2), centrifugation (3), dilution (4-12), dialysis (13), removal of lysozyme prior to precipitation (14), gel-filtration (15), and KC1 extraction (16) yielded preparations with varying chemical and physical properties. The procedures most effective for preparation of an ovomucin free of contamination appear to be density gradient cen- trifugation (17), KCl extraction (16) and dialysis precipitation followed by gel-filtration (18). Even in these preparations, the glycoprotein obtained was found to be heterogeneous by electro- phoresis (18) and sedimentation velocity experiments (17). This heterogeneity may be due to differences in the protein or carbohy- drate moieties of the various fractions, or both.In this study, the carbohydrate portion of ovomucin was examined to determine whether it contributes to the heterogeneity of the glycoprotein. Ovomucin was precipitated by dilution, followed by agarose gel-filtration in the presence of guanidine hydrochloride. The major criteria of purity were molecular weight, sialic acid con- tent and disc polyacrylamide gel electrophoresis using selective staining with Alcian Blue dye and the absence of Amido Black staining bands in the same gel.

Subject Area

Biochemistry|Biology

Recommended Citation

ALMAZAN, AUREA MALABAG, "Characterization of Some Glycopeptides of Ovomucin." (1974). ETD collection for University of Nebraska-Lincoln. AAI7423864.
https://digitalcommons.unl.edu/dissertations/AAI7423864

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