کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1974730 | 1060374 | 2008 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Characterization of the hemoglobins of the neonatal brushtailed possum Trichosurus vulpecula (Kerr): Evidence for a highly cooperative, aggregated isoform of hemoglobin Characterization of the hemoglobins of the neonatal brushtailed possum Trichosurus vulpecula (Kerr): Evidence for a highly cooperative, aggregated isoform of hemoglobin](/preview/png/1974730.png)
The red blood cells of the neonatal brushtailed possum exhibit unusually strong cooperativity at high levels of oxygen saturation (n = 5.4) which appear to arise from a concentration dependent aggregation of one of the neonatal hemoglobin isoforms. Red blood cells from neonatal pouched young exhibit a Bohr factor of − 0.36. Stripped hemolysate is sensitive to added 2,3-bisphosphoglycerate (BPG) (apparent binding constant K = 35 μmol L− 1) and ATP (K = 180 μmol L− 1), but is largely insensitive towards chloride ions. Five isoforms of non-adult hemoglobin were identified using isoelectric focusing. Mass spectrometry indicated that two early isoforms contain alpha chains identical to the adult alpha chain. The remaining three isoforms are composed of identical alpha type and beta type gene products, but differ in their isoelectric points due to differential post-translational modification.
Journal: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology - Volume 150, Issue 1, May 2008, Pages 52–57