% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Artmann:4701,
author = {Artmann, G.M. and Digel, I. and Zerlin, K.F. and
Maggakis-Kelemen, Ch. and Linder, Pt. and Porst, D. and
Stadler, A.M. and Kayser, P. and Dikta, G. and Temiz
Artmann, A.},
title = {{H}emoglobin senses body temperature},
journal = {European biophysics journal},
volume = {38},
issn = {0175-7571},
address = {Berlin},
publisher = {Springer},
reportid = {PreJuSER-4701},
pages = {589 - 600},
year = {2009},
note = {This work was supported by the Ministry of Innovation,
Science, Research and Technology of the State of North
Rhine-Westphalia to G. M.},
abstract = {When aspirating human red blood cells (RBCs) into 1.3 mum
pipettes (DeltaP = -2.3 kPa), a transition from blocking the
pipette below a critical temperature T(c) = 36.3 +/- 0.3
degrees C to passing it above the T(c) occurred
(micropipette passage transition). With a 1.1 mum pipette no
passage was seen which enabled RBC volume measurements also
above T(c). With increasing temperature RBCs lost volume
significantly faster below than above a T(c) = 36.4 +/- 0.7
(volume transition). Colloid osmotic pressure (COP)
measurements of RBCs in autologous plasma (25 degrees C < or
= T < or = 39.5 degrees C) showed a T (c) at 37.1 +/- 0.2
degrees C above which the COP rapidly decreased (COP
transition). In NMR T(1)-relaxation time measurements, the
T(1) of RBCs in autologous plasma changed from a linear (r =
0.99) increment below T(c) = 37 +/- 1 degrees C at a rate of
0.023 s/K into zero slope above T(c) (RBC T(1) transition).
In conclusion: An amorphous hemoglobin-water gel formed in
the spherical trail, the residual partial sphere of the
aspirated RBC. At T(c), a sudden fluidization of the gel
occurs. All changes mentioned above happen at a distinct
T(c) close to body temperature. The T(c) is moved +0.8
degrees C to higher temperatures when a D(2)O buffer is
used. We suggest a mechanism similar to a "glass transition"
or a "colloidal phase transition". At T(c), the stabilizing
Hb bound water molecules reach a threshold number enabling a
partial Hb unfolding. Thus, Hb senses body temperature which
must be inscribed in the primary structure of hemoglobin and
possibly other proteins.},
keywords = {Body Temperature / Erythrocyte Volume / Hemoglobins:
chemistry / Hemoglobins: metabolism / Humans / Magnetic
Resonance Spectroscopy / Osmotic Pressure / Phase Transition
/ Temperature / Water: metabolism / Hemoglobins (NLM
Chemicals) / Water (NLM Chemicals) / J (WoSType)},
cin = {ISB-2},
ddc = {570},
cid = {I:(DE-Juel1)ISB-2-20090406},
pnm = {Programm Biosoft},
pid = {G:(DE-Juel1)FUEK443},
shelfmark = {Biophysics},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:19238378},
UT = {WOS:000265917300005},
doi = {10.1007/s00249-009-0410-8},
url = {https://juser.fz-juelich.de/record/4701},
}