This report describes the use of affinity chromatography on Sepharose-bound concanavalin A for the purification of horseradish peroxidase. Samples of horseradish peroxidase with A .,03:A280 ratios ranging from 0.62 to 2.45 were purified to AIOa:AZSO ratios ranging from approximately 2.8 to 3.1 with
Affinity chromatography on concanavalin a-sepharose of antigenic fractions of human seminal plasma
✍ Scribed by María N. Mazzini; Alberto S. Cerezo; Josefina M.S. de Cerezo
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 569 KB
- Volume
- 173
- Category
- Article
- ISSN
- 1873-3778
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✦ Synopsis
Elution diagrams obtained on affinity chromatography show that the antigenic fractions of human seminal plasma studied, namely (a) the non-diakzable components of human seminal plasma and (b) its trichloroacetic acid-soluble fraction, (c) the trichloroacetic acid-soluble fraction of whole human seminal plasma and (d) the pronase digested human seminal plasma, are complex mixtures of glycoprqteins with minor amounts of polysaccharides. Some of these glycoproteins contain significant percentages of carbohydrates while others contain only trace amounts. Most of the glycoproteins carry non-reducin, = end-chain groups comprising a-D-glucopyranosyl, a-n-mannopyranosyl or sterically related residues.
& 'isma. The substances were then examined by chemical and physicochemical methods l To whom correspondence should be addressed.
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