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Hemoglobin (haemoglobin, Hb or Hgb) is a
protein containing iron that
facilitates the
transportation of
oxygen in red
blood cells.
Almost all vertebrates...
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stimulant use, or anemia, and is the
result of a
reduced amount of
oxyhaemoglobin and may also be
visible as
pallor of the
conjunctivae of the eyes on...
- to
determine hemoglobin concentration,
regardless of its saturation.
Oxyhaemoglobin and
deoxyhaemoglobin have (not exclusively)
isosbestic points at 586 nm...
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change of
primary sequence, H → Y.
Tyrosine stabilizes the Fe(III) form (
oxyhaemoglobin)
creating a
permanent T-state of Hb. Others: High altitude, cyanosis...
- UniProt-Information
about bisphosphoglycerate mutase A live
model of the
effect of
changing 2,3-bisphosphoglycerate on the
oxyhaemoglobin saturation curve...
- Investigation. 58 (6): 459–67. doi:10.1080/00365519850186256. PMID 9832337. A live
model of the
effect of
changing 2,3 BPG on the
oxyhaemoglobin saturation curve...
-
oxygen saturation (SpO2)
drops to 90% or below. This is due to the
oxyhaemoglobin dissociation curve.
Saturations above 90%
produce very
little effect...
- storage,
resulting in
smooth muscle contraction of
cerebral arteries.
Oxyhaemoglobin in
cerebrospinal fluid (CSF)
causes vasoconstriction by
increasing free...
- PMID 16169070. S2CID 8235923.
Shaanan B (1983). "Structure of
human oxyhaemoglobin at 2.1 A resolution". J. Mol. Biol. 171 (1). England: 31–59. doi:10...
- –
insulin dimer, trypsin-pancreatic
trypsin inhibitor complex, and
oxyhaemoglobin –
Cyrus Chothia and Joel
Janin found that
between 1,130 and 1,720 Å2...
