k-Casein which was electrophoretically (Starch gel) homogeneous was hydrolyzed with the enzyme Pronase P and the resultant hydrolyzate was fractionated by column chromatography. A fraction, rich in carbohydrate, was isolated by use of Sephadex G-25. Analysis showed that it contained at least nine different components. Another fraction was isolated by use of Sephadex G-50. Chromatographic, electrophoretic and ultracentrifugal analysis indicated that this fraction contained a single glycopeptide. The glycopeptide contained galactosamine (25.1%), galactose (22.1%) and sialic acid (16.6%), it has no N-term1nal amino acid and has serine as the C-terminal amino acid. Calculation based on the numbers of amino acid residues showed that the molecular weight of the glycopeptide was 11,300. [...]
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.47655 |
| Date | January 1965 |
| Creators | Hwang, Pei-chu. |
| Contributors | B. E. Baker (Supervisor), Baker, B. (Supervisor) |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Master of Science (Department of Agricultural Chemistry) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 000595156, proquestno: AAIMK00549, Theses scanned by UMI/ProQuest. |
Page generated in 0.0021 seconds