Date of Award:

5-1976

Document Type:

Thesis

Degree Name:

Master of Science (MS)

Department:

Wildland Resources

Department name when degree awarded

Wildlife Science

Committee Chair(s)

Clair B. Stalnaker

Committee

Clair B. Stalnaker

Committee

Larre N. Egbert

Committee

Thomas M. Farley

Abstract

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.

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