Thermostability of fish hemoglobins

Borgese, Thomas A.; Harrington, John P.; Borgese, Joan M; Nagel, Ronald L.

doi:10.1016/0305-0491(82)90004-9

Cited by 1 publication

(8 citation statements)

References 17 publications

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“…The description of Type IV haemoglobins as unstable at all pH's is somewhat misleading. It is true that compared with Types I-III they are generally unstable but, as is clear from Borgese et al (1982; Fig. 1B), they are considerably less stable under acid conditions.…”

Section: Buffersmentioning

confidence: 90%

“…Most of the fish they examined fitted into this category. Experiments in the present study were conducted under similar conditions to those of Borgese et al (1982) and it is clear that, using the 60 min criterion for stability, all species except Rhigophila dearborni fit into Type IV. There was insufficient blood from Rhigophila for a prolonged trial at all pH's, but at pH 8.0 there was still 70O7o haemoglobin present after 100 min.…”

Section: Buffersmentioning

confidence: 97%

“…The temperature giving 50°70 denaturation after a four-minute incubation period was 60.0+4.3°C for five species. Borgese et al (1982) looked more closely at thermostability in a range of marine fish and were able to categorise the haemoglobins into four types according to their stability under different conditions. A stable haemoglobin was defined as one in which the time taken for denaturation of 50°7o of the haemoglobin is greater than 60 min.…”

Section: Buffersmentioning

confidence: 99%

“…The method was modified from Borgese et al (1982). An appropriate volume of stock Hb solution was diluted with an equal volume of one of five phosphate buffers.…”

Section: Heat Denaturationmentioning

confidence: 99%

“…The affinity of these haemoglobins for oxygen is lower than that predicted by Van't Hoff temperature projections (Wells and Jokumsen 1982) which accords with open molecular structures for function at low temperatures. In the present study we examine the thermostability of the haemoglobin from Antarctic teleosts for comparison with data from temperate species (see Borgese et al 1982).…”

Section: Introductionmentioning

confidence: 99%

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Thermostability of haemoglobins from Antarctic fish

Warren

Wells

1988

Polar Biol

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Summary.Proteins from Antarctic fish are less stable at high temperatures than those from fish from lower latitudes. Investigations into the thermostability of haemoglobins from a range of Antarctic teleosts have been carried out for comparison with data from temperate species. Haemoglobin concentrations following periods of heating at 50°C were analysed spectrophotometrically and the time taken for 50°70 denaturation (t50%) determined. The effects of pH and salt concentrations were also examined. With the exception of that of Rhigophila dearborni, the haemoglobins were found to be relatively unstable with ts0 % values ranging from 7.7 to 29.9 min at pH 7. All haemoglobins became less stable on addition of KC1 but the effect of pH was variable. Freezing had no effect on the stability of haemoglobin from Dissostichus mawsoni. The thermostability of haemoglobin from a temperate nototheniid, Notothenia angustata, was within the range displayed by its Antarctic relatives and it would seem that in general the differences between genera are as great as those between Antarctic and temperate species as a whole.

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Section: Buffersmentioning

confidence: 90%

Section: Buffersmentioning

confidence: 97%

Section: Buffersmentioning

confidence: 99%

“…The method was modified from Borgese et al (1982). An appropriate volume of stock Hb solution was diluted with an equal volume of one of five phosphate buffers.…”

Section: Heat Denaturationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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