A comparative study of the respiratory properties and physiological function of haemocyanin in two burrowing and two non-burrowing crustaceans

Structural and functional properties of hemocyanin from Cyanagraea praedator, a deep‐sea hydrothermal vent crab

“…This cofactor, which binds preferentially on oxyhemocyanin, increases the Hc‐O 2 affinity in most cases 7. For many decapod species, the lactate effect varies between −0.09 and −0.6 and increases with pH 13. However, for C. praedator, lactate has an effect neither on affinity nor on the Bohr effect.…”

“…Several cofactors are known to modify Hc‐O 2 affinity, such as lactate11 or urate,12 which increase affinity. A temperature increase is the most common inducer of an affinity decrease 13, 14. The Bohr coefficient is normal and large for brachyuran species 7, 15.…”

Structural and functional properties of hemocyanin from Cyanagraea praedator, a deep‐sea hydrothermal vent crab

“…This cofactor, which binds preferentially on oxyhemocyanin, increases the Hc‐O 2 affinity in most cases 7. For many decapod species, the lactate effect varies between −0.09 and −0.6 and increases with pH 13. However, for C. praedator, lactate has an effect neither on affinity nor on the Bohr effect.…”

“…Several cofactors are known to modify Hc‐O 2 affinity, such as lactate11 or urate,12 which increase affinity. A temperature increase is the most common inducer of an affinity decrease 13, 14. The Bohr coefficient is normal and large for brachyuran species 7, 15.…”

Temperature Sensitivity of Molluscan and Arthropod Hemocyanins

“…(1985) and Sanders and Childress (1985) both reported decreases in the 2 affinity of other crustacean Hcs at low temperature. As is also true of most other 2 carriers, temperature sensitivity of Hc0 2 affinity varies within a species, often becoming smaller as temperature rises (Mauro and Mangum, 1982a, b;Bridges, 1986). In at least two species of terrestrial crustaceans, however, the temperature sensitivity of HcO : affinity is smallest in the temperature range in which the animals live Bridges, 1985, 1986).…”

Adaptations to the Deep-Sea Oxygen Minimum Layer: Oxygen Binding by the Hemocyanin of the Bathypelagic Mysid, Gnathophausia ingens Dohrn

“…In fact, shallow-dwelling crustaceans living at lower temperatures have hemocyanins with lower Oi affinities as well as lower cooperativities, presumably to maintain a sufficient unloading of O : to their tissues (Redmond, 1968;Mangum, 1982;Mauro and Mangum 1982a). In addition, the temperature sensitivity of O : binding by hemocyanin is often greater at lower temperatures (Mauro and Mangum, 1982b;Bridges, 1986;Burnett el <//.. 1988). The hemocyanin of G. ingens also seems to have subunits that are quite different electrophoretically from those of decapods (J. E. Reese and C. P. Mangum, pers.…”

“…Although the O : binding properties of the hemocyanins of crustaceans inhabiting sometimes hypoxic environments are well studied (Mangum, 1980;Mangum 1983a,b;Taylor, 1983, 1985;Bridges, 1986), the deep-sea oxygen minima are unique in having stable low oxygen conditions in combination with constant low temperatures. Gnathophausia ingens, like most midwater crustaceans, is denser than seawater (Childress and Nygaard, 1974).…”

Structural and functional properties of hemocyanin from Cyanagraea praedator, a deep‐sea hydrothermal vent crab

“…This cofactor, which binds preferentially on oxyhemocyanin, increases the Hc‐O 2 affinity in most cases 7. For many decapod species, the lactate effect varies between −0.09 and −0.6 and increases with pH 13. However, for C. praedator, lactate has an effect neither on affinity nor on the Bohr effect.…”

“…Several cofactors are known to modify Hc‐O 2 affinity, such as lactate11 or urate,12 which increase affinity. A temperature increase is the most common inducer of an affinity decrease 13, 14. The Bohr coefficient is normal and large for brachyuran species 7, 15.…”

Temperature Sensitivity of Molluscan and Arthropod Hemocyanins

“…(1985) and Sanders and Childress (1985) both reported decreases in the 2 affinity of other crustacean Hcs at low temperature. As is also true of most other 2 carriers, temperature sensitivity of Hc0 2 affinity varies within a species, often becoming smaller as temperature rises (Mauro and Mangum, 1982a, b;Bridges, 1986). In at least two species of terrestrial crustaceans, however, the temperature sensitivity of HcO : affinity is smallest in the temperature range in which the animals live Bridges, 1985, 1986).…”

Adaptations to the Deep-Sea Oxygen Minimum Layer: Oxygen Binding by the Hemocyanin of the Bathypelagic Mysid, Gnathophausia ingens Dohrn

“…In fact, shallow-dwelling crustaceans living at lower temperatures have hemocyanins with lower Oi affinities as well as lower cooperativities, presumably to maintain a sufficient unloading of O : to their tissues (Redmond, 1968;Mangum, 1982;Mauro and Mangum 1982a). In addition, the temperature sensitivity of O : binding by hemocyanin is often greater at lower temperatures (Mauro and Mangum, 1982b;Bridges, 1986;Burnett el <//.. 1988). The hemocyanin of G. ingens also seems to have subunits that are quite different electrophoretically from those of decapods (J. E. Reese and C. P. Mangum, pers.…”

“…Although the O : binding properties of the hemocyanins of crustaceans inhabiting sometimes hypoxic environments are well studied (Mangum, 1980;Mangum 1983a,b;Taylor, 1983, 1985;Bridges, 1986), the deep-sea oxygen minima are unique in having stable low oxygen conditions in combination with constant low temperatures. Gnathophausia ingens, like most midwater crustaceans, is denser than seawater (Childress and Nygaard, 1974).…”

Structural and functional properties of hemocyanin from Cyanagraea praedator, a deep‐sea hydrothermal vent crab

“…This cofactor, which binds preferentially on oxyhemocyanin, increases the Hc‐O 2 affinity in most cases 7. For many decapod species, the lactate effect varies between −0.09 and −0.6 and increases with pH 13. However, for C. praedator, lactate has an effect neither on affinity nor on the Bohr effect.…”

“…Several cofactors are known to modify Hc‐O 2 affinity, such as lactate11 or urate,12 which increase affinity. A temperature increase is the most common inducer of an affinity decrease 13, 14. The Bohr coefficient is normal and large for brachyuran species 7, 15.…”

Temperature Sensitivity of Molluscan and Arthropod Hemocyanins

“…(1985) and Sanders and Childress (1985) both reported decreases in the 2 affinity of other crustacean Hcs at low temperature. As is also true of most other 2 carriers, temperature sensitivity of Hc0 2 affinity varies within a species, often becoming smaller as temperature rises (Mauro and Mangum, 1982a, b;Bridges, 1986). In at least two species of terrestrial crustaceans, however, the temperature sensitivity of HcO : affinity is smallest in the temperature range in which the animals live Bridges, 1985, 1986).…”

Adaptations to the Deep-Sea Oxygen Minimum Layer: Oxygen Binding by the Hemocyanin of the Bathypelagic Mysid, Gnathophausia ingens Dohrn

“…In fact, shallow-dwelling crustaceans living at lower temperatures have hemocyanins with lower Oi affinities as well as lower cooperativities, presumably to maintain a sufficient unloading of O : to their tissues (Redmond, 1968;Mangum, 1982;Mauro and Mangum 1982a). In addition, the temperature sensitivity of O : binding by hemocyanin is often greater at lower temperatures (Mauro and Mangum, 1982b;Bridges, 1986;Burnett el <//.. 1988). The hemocyanin of G. ingens also seems to have subunits that are quite different electrophoretically from those of decapods (J. E. Reese and C. P. Mangum, pers.…”

“…Although the O : binding properties of the hemocyanins of crustaceans inhabiting sometimes hypoxic environments are well studied (Mangum, 1980;Mangum 1983a,b;Taylor, 1983, 1985;Bridges, 1986), the deep-sea oxygen minima are unique in having stable low oxygen conditions in combination with constant low temperatures. Gnathophausia ingens, like most midwater crustaceans, is denser than seawater (Childress and Nygaard, 1974).…”