Results 341 to 350 of about 23,660,822 (374)
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Spectroscopy of Single Hemoglobin Molecules by Surface Enhanced Raman Scattering
, 1999We demonstrate the detection of molecular vibrations in single hemoglobin (Hb) protein molecules attached to isolated and immobilized silver nanoparticles by surface enhanced Raman scattering (SERS).
Hongxing Xu +3 more
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Racial Differences in the Relationship of Glucose Concentrations and Hemoglobin A1c Levels.
Annals of Internal Medicine, 2017Background Debate exists as to whether the higher hemoglobin A1c (HbA1c) levels observed in black persons than in white persons are due to worse glycemic control or racial differences in the glycation of hemoglobin.
R. Bergenstal +23 more
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, 2007
The American College of Physicians’ Clinical Efficacy Assessment Subcommittee reviewed the strengths and weaknesses of guidelines from nine ...
R. Saitz, Facp., Fasam
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The American College of Physicians’ Clinical Efficacy Assessment Subcommittee reviewed the strengths and weaknesses of guidelines from nine ...
R. Saitz, Facp., Fasam
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Combined Fenton and starvation therapies using hemoglobin and glucose oxidase.
Nanoscale, 2019Separately, Fenton and starvation cancer therapies have been recently reported as impressive methods for tumor destruction. Here, we introduce natural hemoglobin and glucose oxidase (GOx) for efficient cancer treatment following combined Fenton and ...
H. Ranji-Burachaloo +4 more
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Archives of Biochemistry and Biophysics, 1977
Abstract Transverse water proton relaxation times ( T 2 ) have been measured as a function of time after deoxygenation of solutions containing hemoglobin S. The shortened T 2 values observed upon deoxygenation of hemoglobin S result from an increase in the correlation time ( τ c ) of the water fraction irrotationally bound to deoxyhemoglobin S ...
Waterman Mr +5 more
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Abstract Transverse water proton relaxation times ( T 2 ) have been measured as a function of time after deoxygenation of solutions containing hemoglobin S. The shortened T 2 values observed upon deoxygenation of hemoglobin S result from an increase in the correlation time ( τ c ) of the water fraction irrotationally bound to deoxyhemoglobin S ...
Waterman Mr +5 more
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Anemia in Clinical Practice-Definition and Classification: Does Hemoglobin Change With Aging?
Seminars in hematology (Print), 2015Anemia is a global public health problem affecting both developing and developed countries at all ages. According to the World Health Organization (WHO), anemia is defined as hemoglobin (Hb) levels
M. Cappellini, I. Motta
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2003
Publisher Summary This chapter describes the chemical approaches of protein engineering that are amenable to the generation of mutants of hemoglobin (Hb). The need and significance of the chemical approaches of protein engineering in this era of oligonucleotide-directed site-specific mutagenesis are also emphasized.
Sonati Srinivasulu +1 more
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Publisher Summary This chapter describes the chemical approaches of protein engineering that are amenable to the generation of mutants of hemoglobin (Hb). The need and significance of the chemical approaches of protein engineering in this era of oligonucleotide-directed site-specific mutagenesis are also emphasized.
Sonati Srinivasulu +1 more
openaire +3 more sources
American Scientist, 1999
The appearance of atmospheric oxy gen on earth b tween one and two billion years ago was a dramatic and, for the primitive single-celled creatures then living on earth, a potentially trau matic event. On the one hand, oxygen was toxic. On the other hand, oxygen presented opportunities to improve the process of metabolism, increasing the efficiency of ...
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The appearance of atmospheric oxy gen on earth b tween one and two billion years ago was a dramatic and, for the primitive single-celled creatures then living on earth, a potentially trau matic event. On the one hand, oxygen was toxic. On the other hand, oxygen presented opportunities to improve the process of metabolism, increasing the efficiency of ...
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2014
This chapter is a brief overview of hemoglobin (Hgb), which is the protein in blood that is rich in iron and gives it the red color. It makes up about 95% of a red blood cell and has an oxygen-binding capacity of 1.34 mL O2/g, which satisfies the need for the average adult consumption of 250 mL of oxygen per minute.
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This chapter is a brief overview of hemoglobin (Hgb), which is the protein in blood that is rich in iron and gives it the red color. It makes up about 95% of a red blood cell and has an oxygen-binding capacity of 1.34 mL O2/g, which satisfies the need for the average adult consumption of 250 mL of oxygen per minute.
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LINKED FUNCTIONS AND RECIPROCAL EFFECTS IN HEMOGLOBIN: A SECOND LOOK.
Advances in Protein Chemistry, 1964J. Wyman
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