Nine hemoglobins from adult rainbow trout have been isolated by starch gel electrophoresis using a Trisborate buffer system, pH 8.7. Six fast and two slow anodally migrating hemoglobins, and one slow cathodally migrating hemoglobin were observed in all specimens.
The nine hemoglobins have been purified by DEAE cellulose ion exchange chromatography followed by starch gel electrophoresis.
The subunit structure of each purified hemoglobin has been partially examined by gel electrofocusing (GEF) in .5 percent polyacrylamide gels containing 8M urea and lmM dithiothereitol (DTT). Tetrameric combinations of one, two, three, and four polypeptide chains are present.
Twelve hemoglobins have been isolated from cutthroat trout. Six fast and two slow anodally migrating hemoglobins, and four cathodally migrating hemoglobins were observed in most of the specimens.
Hemoglobin polymorphism has been detected in a population of Yellowstone Lake cutthroat trout, Yellowstone Park, Wyoming. Six phenotypic patterns were evident.
| Identifer | oai:union.ndltd.org:UTAHS/oai:digitalcommons.usu.edu:etd-5980 |
| Date | 01 May 1976 |
| Creators | Braman, Jeffrey Carl |
| Publisher | DigitalCommons@USU |
| Source Sets | Utah State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | All Graduate Theses and Dissertations |
| Rights | Copyright for this work is held by the author. Transmission or reproduction of materials protected by copyright beyond that allowed by fair use requires the written permission of the copyright owners. Works not in the public domain cannot be commercially exploited without permission of the copyright owner. Responsibility for any use rests exclusively with the user. For more information contact Andrew Wesolek (andrew.wesolek@usu.edu). |
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