Oxygen binding by the hemocyanin of Busycon canaliculatum |
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| Institution: | 1. Centre for Wildlife Ecology, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada;2. US Geological Survey, Alaska Science Center, 4210 University Drive, Anchorage, AK 99508, USA;3. Science and Technology Branch, Environment and Climate Change Canada, 5421 Robertson Road, Delta, BC V4K 3N2, Canada;4. Stantec Consulting Ltd., 2042 Mills Rd W, Sidney, BC V8L 5X4, Canada;5. Centre for Wildlife Ecology, Simon Fraser University, 8888 University Drive, Burnaby, BC V5A 1S6, Canada |
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| Abstract: | - 1.1. This study examined the effect of the monoamines dopamine and octopamine, as well as tyrosine on the oxygen affinity and cooperativity of oxygen binding by the hemocyanin of the marine gastropod Busycon canaliculatum. The effect of temperature on hemocyanin oxygen affinity was also examined.
- 2.2. Freezing Busycon hemocyanin did not affect the binding of oxygen.
- 3.3. Dopamine, octopamine and tyrosine had no significant effect on the oxygen affinity or cooperativity of oxygen binding by the hemocyanin of B. canaliculatum.
- 4.4. It was concluded that Busycon hemocyanin either has no binding sites for the two monoamines or for tyrosine, or that binding of the molecules has no functional significance.
- 5.5. Both temperature sensitivity and affinity of hemocyanin-oxygen binding were similar to values previously reported for hemocyanin of Busycon from other localities.
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