Results 161 to 170 of about 24,139 (199)

Microvascular Consequences of Methemoglobin Compared to Reduced Hemoglobin in the Microcirculation. [PDF]

Microcirculation
Martinez J, Munoz C, Lucas D, Muller C, Govender K, Gu X, Palmer AF, Cabrales P.   +7 more
europepmc   +1 more source

Use of Topical Nitroglycerin in the Treatment of Acute Limb Ischemia: Four-Year Experience in a Mixed Neonatal and Pediatric Intensive Care Unit. [PDF]

J Mother Child
Jesus AR, Fradique AR, Teixeira C, Carvalho L, Dionísio T.   +4 more
europepmc   +1 more source

Severe Methemoglobinemia Following Alkyl Nitrite Ingestion: A Case Report. [PDF]

Cureus
Kalik Z, Momoh R.
europepmc   +1 more source

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Primaquine and methemoglobin

Clinical Pharmacology & Therapeutics, 1964
Methemoglobin formation occurring as a toxic manifestation of primaquine was studied in volunteers to determine whether or not it is an example of genetic polymorphism. No evidence of polymorphism was found.
W K, COWAN, D A, EVANS
openaire   +2 more sources

Photochemical reduction of methemoglobin and methemoglobin derivatives

Free Radical Biology and Medicine, 1990
Publisher Summary Hemoglobin solutions that must be stored for long periods of time must be kept either at very low temperatures or in the complete absence of oxygen, or both. These are conditions are not easy to achieve. The spontaneous oxidation to methemoglobin can be especially bothersome when solutions of precious hemoglobin variants or ...
openaire   +2 more sources

Structure of azide methemoglobin

Journal of Molecular Biology, 1979
Abstract We have compared the structures of horse azide methemoglobin and methemoglobin (MetHb) at 2.8 A resolution by X-ray difference Fourier analysis. Of four low-spin liganded Hb derivatives (nitric oxide Hb, carbon monoxide Hb, cyanide MetHb, and azide MetHb), azide MetHb is closest in structure to MetHb.
J F, Deatherage, S K, Obendorf, K, Moffat   +2 more
openaire   +2 more sources

Structure of fluoride methemoglobin

Journal of Molecular Biology, 1976
Abstract The structures of fluoride methemoglobin and acid methemoglobin have been compared by X-ray difference Fourier techniques. Despite the close similarity in ligand bulk and iron spin in these complexes, small but significant differences in tertiary structure are found. The globin structure is clearly extremely sensitive to small changes in the
J F, Deatherage, R S, Loe, K, Moffat
openaire   +2 more sources