Calibration of the HemoCue point-of-care analyser for determining haemoglobin concentration in a lizard and a fish (original) (raw)
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Calibration of a hand-held haemoglobin analyser for use on fish blood
Journal of Fish Biology, 2008
The HemoCue haemoglobin analyser consistently overestimated haemoglobin concentration ([Hb]) in the blood of all fish species (sockeye salmon Oncorhynchus nerka, Chinook salmon Oncorhynchus tshawytscha, Pacific bluefin tuna Thunnus orientalis and chub mackerel Scomber japonicus) by 22-50% (9Á9-36Á0 g l À1) over a [Hb] range of 20-160 g l À1. The systematic nature of the overestimation, however, allowed the formulation of an accurate calibration equation that can be used to correct values of [Hb] measured by the HemoCue in field studies.
Brazilian Journal of Medical and Biological Research, 2007
Vertebrate hemoglobin, contained in erythrocytes, is a globular protein with a quaternary structure composed of 4 globin chains (2 alpha and 2 beta) and a prosthetic group named heme bound to each one. Having myoglobin as an ancestor, hemoglobin acquired the capacity to respond to chemical stimuli that modulate its function according to tissue requirements for oxygen. Fish are generally submitted to spatial and temporal O 2 variations and have developed anatomical, physiological and biochemical strategies to adapt to the changing environmental gas availability. Structurally, most fish hemoglobins are tetrameric; however, those from some species such as lamprey and hagfish dissociate, being monomeric when oxygenated and oligomeric when deoxygenated. Fish blood frequently possesses several hemoglobins; the primary origin of this finding lies in the polymorphism that occurs in the globin loci, an aspect that may occasionally confer advantages to its carriers or even be a harmless evolutionary remnant. On the other hand, the functional properties exhibit different behaviors, ranging from a total absence of responses to allosteric regulation to drastic ones, such as the Root effect.
Biochimica et biophysica acta, 1976
Blood from the primitive holostean fish, the bowfin, Amia calva, contains 2 mo of ATP per mol of hemoglobin. The hemolysates contain at least five tetrameric hemoglobin components which differ in their oxygen affinities and their response to cofactors such as ATP. The binding of oxygen by each chromatographically isolated component, including a cathodal component, is influenced by pH and organic phosphates; there is no significant differentiation of function or structure as seen in trout and certain other fish hemolysates. Kinetic analyses of ligand binding indicate that the Bohr and Root effects of Amia calva hemoglobins are best explained by changes in both the "on" and "off" constants. At low pH, the increase in the "off" constant is smaller than for most other Root hemoglobins. The hemoglobin system of Amina calva is functionally undifferentiated and may be representative of the ancestral condition in teleosts.
Studies of the hemoglobins of the eel (Anguilla anguilla L.)—I
Comparative Biochemistry and Physiology Part A: Physiology, 1980
Stripped eel erythrolysate shows low buffer capacity, similar to the low buffer capacity of whole eel blood. 2. O2 and CO binding at 100 kPa each shows a high fixed-acid Haldane effect, though lower in the case of O2 binding where the saturation is incomplete due to the Root effect. 3. GTP, ATP and IHP have little effect on the CO-induced fixed-acid Haldane effect. 4. Generally two, in few cases three, main eel hemoglobin components were isolated: HbE, and HbE, (the latter being the Root effect hemoglobin). 5. Spectra of deoxy, oxy and carboxy derivatives of these hemoglobins are very similar, though slightly red-shifted in HbE, with respect to HbEi. 6. HbE, and HbE2 contain 0 and 6 titratable sulphhydryl groups respectively.
Comparative Analysis of Human and Porcupine (Hystrix Cristata L., 1758) Haemoglobins
2008
Agarose gel electrophoresis was used to determine the electrophoretic pattern of the haemoglobin of Hystrix cristata (H. cristata), and that of a healthy human. Alkaline agarose gel electrophoresis of the haemoglobin of H. cristata revealed that the mobility of the H. cristata haemoglobin was considerably faster than that of human haemoglobin. These comparisons showed obvious differences between the haemoglobin of the two species.