Results 1 to 10 of about 9,818 (189)
rTMS Therapy Reduces Hypofrontality in Patients With Depression as Measured by fNIRS
Frontiers in Psychiatry, 2022 Multichannel functional near-infrared spectroscopy (fNIRS) is a tool used to capture changes in cerebral blood flow. A consistent result for depression is a decrease in blood flow in the frontal cortex leading to hypofrontality, which indicates ...
Yasuo Kawabata +10 more
doaj +1 more source
Chinese Journal of Contemporary Neurology and Neurosurgery, 2022 Objective To investigate the changes of brain activation and brain network connectivity in patients with spinal cord injury (SCI). Methods A total of 20 patients with SCI were selected from Qilu Hospital of Shandong University from January to October ...
SUN Zhi⁃fang +4 more
doaj +1 more source
Transnitrosation Signals Oxyhemoglobin Desaturation [PDF]
Circulation Research, 2008 See related article, pages 545–553 Erythrocytes dilate peripheral blood vessels as a function of oxyhemoglobin desaturation.1 This effect increases regional blood flow to hypoxic tissues. The mechanisms underlying the peripheral vasodilatory effects of desaturating erythrocytes are incompletely understood but do not involve activation of local ...
Nadzeya, Marozkina +2 more
openaire +2 more sources
Magnetic properties of oxyhemoglobin. [PDF]
Proceedings of the National Academy of Sciences, 1977 When the magnetic susceptibility of frozen aqueous solutions of human oxyhemoglobin was measured in the range between 25 and 250 K, it showed a temperature-dependent behavior typical of a thermal equilibrium between a ground singlet state and an excited triplet state for two electrons per heme, the energy separation being [2J] = 146 cm-1.
Cerdonio M +5 more
openaire +3 more sources
DIFFERENTIATION OF OXYHEMOGLOBINS BY MEANS OF MUTUAL SOLUBILITY TESTS
The Journal of General Physiology, 1923 1. The rule of addition of solubilities is applicable to the differentiation of the oxyhemoglobins of not too closely related species. 2. The oxyhemoglobins of the horse, dog, rat, and guinea pig show differences when tested by this method.
K. Landsteiner, M. Heidelberger
semanticscholar +1 more source
The kinetics of assembly of normal and variant human oxyhemoglobins.
Journal of Biological Chemistry, 1987 The kinetics of assembly have been monitored spectrophotometrically for normal and variant human oxyhemoglobins in 0.1 M Tris, 0.1 M NaCl, 1 mM Na2EDTA, pH 7.4, at 21.5 degrees C.
Human Oxyhemoglobins +7 more
semanticscholar +1 more source
The dissociation of the first oxygen molecule from some mammalian oxyhemoglobins.
Journal of Biological Chemistry, 1971 The velocity of dissociation of oxygen from the α and β chains of saturated tetrameric oxyhemoglobin has been measured by detailed analysis of the time course of the replacement of oxygen by carbon monoxide.
J. Olson, M. E. Andersen, Q. Gibson
semanticscholar +1 more source
Journal of Biological Chemistry, 1985 Reactions of human oxyhemoglobin A with iron(II) compounds have been investigated. Human oxyhemoglobin (HbO2) reacts with aquopentacyanoferrate(II), Fe(II)(CN)5H2O3-, to yield hydrogen peroxide, aquomethemoglobin and Fe(III)(CN)5H2O2-.
S. Kawanishi, W. Caughey
semanticscholar +1 more source
Ultrafast Spectroscopy of Oxyhemoglobin during Photodissociation [PDF]
The Journal of Physical Chemistry B, 2010 Ultrafast time-resolved pump-probe spectroscopy was studied to clarify the detailed mechanism in the photodissociation process of oxyhemoglobin in the visible spectral range. The photodissociation had not been time-resolved and only the upper limit of the time needed for the dissociation process was claimed to be faster than 50 fs; it was time-resolved
Atsushi, Yabushita, Takayoshi, Kobayashi
openaire +2 more sources
Exchange of heme among hemoglobins and between hemoglobin and albumin.
Journal of Biological Chemistry, 1968 Intact heme groups undergo exchange between molecules of human hemoglobin under physiological conditions. This phenomenon requires the presence of ferrihemoglobin and is blocked by heme ligands or the prior binding of hemoglobin to haptoglobin.
H. F. Bunn, J. H. Jandl
semanticscholar +1 more source