نتایج جستجو برای: hemoglobins

تعداد نتایج: 1615  

Journal: :International archives of allergy and applied immunology 1986
H Prelicz X Baur M Dewair H Tichy A B Kay R Tee P S Cranston

Chironomid hemoglobins are potent allergens. The allergenic and antigenic activities of these hemoglobins are studied with the help of RAST, RAST inhibition and double immunodiffusion. Human as well as rabbit antisera were used. It was shown that hemoglobins are the main antigenic/allergenic components in extracts of Camptochironomus tentans larvae. Furthermore, immunological cross-reactivity a...

Journal: :Journal of the American Chemical Society 2004
Uri Samuni Yannick Ouellet Michel Guertin Joel M Friedman Syun-Ru Yeh

HbN and HbO are two truncated hemoglobins from Mycobacterium tuberculosis. Resonance Raman spectra of the deoxy derivatives of these two homodimeric hemoglobins indicate that there is no proximal strain imposed by intersubunit interactions on the proximal iron-histidine bond as that observed in the tetrameric human hemoglobin. In addition, with nanosecond laser flash photolysis, it was conclude...

Journal: :Journal of Biological Chemistry 2001

Journal: :The Journal of biological chemistry 1975
E Oldfield A Allerhand

Proton-decoupled natural abundance 13C NMR spectra of carbon monoxide hemoglobins were recorded at 15.18 MHz by the Fourier transform method, under conditions of spectrometer sensitivity sufficient for detection of individual carbon resonances. The aromatic region of each spectrum contains broad bands of methine carbon resonances, and some relatively narrow peaks arising from nonprotonated carb...

Journal: :Brazilian Journal of Medical and Biological Research 2007

2002
ADAM ALLERHAND

Proton-decoupled natural abundance 13C NMR spectra of carbon monoxide hemoglobins were recorded at 15.18 MHz by the Fourier transform method, under conditions of spectrometer sensitivity sufficient for detection of individual carbon resonances. The aromatic region of each spectrum contains broad bands of methine carbon resonances, and some relatively narrow peaks arising from nonprotonated carb...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1970
H Jacob K Winterhalter

Mutant, unstable hemoglobins precipitate as Heinz bodies in circulating red blood cells resulting in their premature hemolysis. We stress that generally these hemoglobins contain amino acid substitutions in the beta-chain of globin near the heme pocket, and demonstrate that heme binding suffers thereby. Four genetically unstable hemoglobins lost roughly half their heme content while precipitati...

Journal: :Journal of Clinical Pathology 1978

2015
Ana B. Christensen Joseph L. Herman Maurice R. Elphick Kord M. Kober Daniel Janies Gregorio Linchangco Dean C. Semmens Xavier Bailly Serge N. Vinogradov David Hoogewijs Hector Escriva

BACKGROUND Recent genomic information has revealed that neuroglobin and cytoglobin are the two principal lineages of vertebrate hemoglobins, with the latter encompassing the familiar myoglobin and α-globin/β-globin tetramer hemoglobin, and several minor groups. In contrast, very little is known about hemoglobins in echinoderms, a phylum of exclusively marine organisms closely related to vertebr...

Journal: :Clinical chemistry 1975
E J Hicks B J Hughes

We compare and discuss three electrophoretic methods for identifying hemoglobins S, A, C, F, and D or G. Electrophoresis on citrate agar gel was more sensitive than electrophoresis on cellulose acetate for detecting hemoglobins S and F, a fundamental consideration in designing cord-blood screening programs for detecting hemoglobin S carriers. Electrophoresis on starch gel is evidently an accept...

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