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Junting Zhang et al.
Analytical and bioanalytical chemistry, 409(18), 4459-4465 (2017-05-21)
Fourier transform infrared (FTIR) spectroscopy is one of the widely used vibrational spectroscopic methods in protein structural analysis. The protein solution sample loaded in demountable CaF
Vladimir M Turzhitsky et al.
Applied optics, 47(32), 6046-6057 (2008-11-13)
There has been significant interest in developing depth-selective optical interrogation of biological tissue in general and of superficial (e.g., mucosal) tissue in particular. We report an in vivo polarization-gating fiber-optic probe that obtains backscattering spectroscopic measurements from a range of
Christos D Georgiou et al.
Redox biology, 17, 236-245 (2018-05-05)
A new fluorometric assay is presented for the ultrasensitive quantification of total protein carbonyls, and is based on their specific reaction with rhodamine B hydrazide (RBH), and the production of a protein carbonyl-RBH hydrazone the fluorescence of which (at ex/em
Yan Zhang et al.
Zoological science, 20(9), 1087-1093 (2003-10-28)
The physiological significance of the position and shape of the oxygen equilibrium curve (OEC) of horse hemoglobin (Hb) is considered from the viewpoint of oxygen (O2) transport efficiency and the effectiveness of the Bohr effect. In horse fetal and maternal
Alain J Marengo-Rowe
Proceedings (Baylor University. Medical Center), 19(3), 239-245 (2007-01-26)
In 1949 Pauling and his associates showed that sickle cell hemoglobin (HbS) belonged to an abnormal molecular species. In 1958 Ingram, who used a two-dimensional system of electrophoresis and chromatography to break down the hemoglobin molecule into a mixture of
Chung-Chieh Yu et al.
Optics express, 16(20), 16227-16239 (2008-10-01)
We report a fully quantitative spectroscopy imaging instrument for wide area detection of early cancer (dysplasia). This instrument provides quantitative maps of tissue biochemistry and morphology, making it a potentially powerful surveillance tool for objective early cancer detection. We describe
D M Villarreal et al.
Applied and environmental microbiology, 74(18), 5854-5856 (2008-08-05)
To produce recombinant hemoglobin in Escherichia coli, sufficient intracellular heme must be present, or the protein folds improperly and is degraded. In this study, coexpression of human hemoglobin genes and Plesiomonas shigelloides heme transport genes enhanced recombinant hemoglobin production in
A comparative study on STM imaging and electrocatalytic activity of different surfaces modified with flavin adenine dinucleotide
Jingdong Zhang, Qijin Chi, Erkang Wang, Shaojun Dong
Electrochimica Acta, 40, 733-744 (1995)
Alan N Schechter
Blood, 112(10), 3927-3938 (2008-11-08)
Much of our understanding of human physiology, and of many aspects of pathology, has its antecedents in laboratory and clinical studies of hemoglobin. Over the last century, knowledge of the genetics, functions, and diseases of the hemoglobin proteins has been
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