QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by WILKES, P.R. H. Articles by McMAHON, B. R. Search for Related Content PubMed Articles by WILKES, P.R. H. Articles by McMAHON, B. R.

Journal of Experimental Biology 98,139-149 (1982)
Published by Company of Biologists 1982

Effect of Maintained Hypoxic Exposure on the Crayfish Orconectes Rusticus: II. Modulation of Haemocyanin Oxygen Affinity

P.R. H. WILKES ¹ and B. R. McMAHON ¹

¹ Department of Biology, University of Calgary Calgary, Alberta, Canada T2N 1N4

Haemolymph Na⁺, Cl^-, K⁺, Mg²⁺, Ca²⁺, Cu²⁺ and protein levels, in vivo postbranchial acid-base status (total CO₂, pH and P_COCO2), in vitro haemolymph buffer value, Bohr value and oxygen affinity were measured before and after a 3-week period in which control crayfish were maintained at normoxia and experimental crayfish were maintained at an ambient oxygen tension of 50-55 torr. Analysis of haemolymph Cu²⁺ and protein levels in control and experimental crayfish indicated no increase in haemocyanin and therefore oxygen carrying capacity of the haemolymph. Although the Bohr value was not significantly different between control and experimental crayfish, the haemocyanin oxygen affinity was elevated in the hypoxic crayfish by two mechanisms. The first was dependent upon the haemolymph H⁺ concentration, i.e. a Bohr shift resulting from a respiratory alkalosis. The second mechanism was independent of haemolymph H⁺ concentration in that at a given pH haemolymph from experimental crayfish had a significantly higher oxygen affinity. The decrease in p₅₀ probably cannot be attributed to a specific cation effect.

This article has been cited by other articles:

				C. Bridges Modulation of haemocyanin oxygen affinity: properties and physiological implications in a changing world J. Exp. Biol., January 3, 2001; 204(5): 1021 - 1032. [Abstract] [PDF]