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These two lines have features that are the most characteristic of human HB and have been widely used in HB-related investigations [ 40, 48].
The molecular weights of human Hb A and Hb F in the CO form were dependent on concentration.
The α2Pβ2S retains normal tetrameric structure (α2β2) of human Hb and an O2 affinity comparable to that of HbS in 50 mM Hepes buffer; but, its O2 affinity is slightly higher than that of HbS in the presence of allosteric effectors (chloride, DPG and phosphate).
A 20 µg/µl stock solution of human Hb which was primarily in the form of metHb (both stated by the manufacturer and confirmed by spectral analysis) was used to make individual 100 µl samples containing 2 mg of Hb.
The Magstream I-FOBT relies on an antibody directed against the globin moiety of human Hb.
Quantitative assessment of human Hb was obtained through an antigen antibody agglutination reaction using human anti-Hb polyclonal antibodies adsorbed on polystyrene particles: agglutination was measured as a 660-nm absorbency increase, proportional to Hb content in tested samples.
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Finally, the strongly suppressed DPG sensitivities of human Hbs with residue replacements at β82 (e.g., Hb Rahere β82Lys→Thr and Hb Providence β82Lys→Asn/Asp; [ 32, 33]) are qualitatively similar in magnitude to that of eastern mole Hb.
To facilitate the study of the structure-function relationship of human hemoglobin (Hb A), we have developed a new hemoglobin expression vector, pGEX6P-α-[SD]-β.
In this paper the corona formation and structural deformation of human hemoglobin (Hb) induced by the assembly on silver nanoparticle (AgNP) surface were studied in time dependent manner by various spectroscopic techniques and electron microscopic method.
Over the past 20 years, an alternative type of FOBT has been developed based on the immunological detection of human haemoglobin (Hb), and offering greater sensitivity for the detection of invasive cancers and pre-neoplastic lesions (Morikawa et al, 2005; Castiglione et al, 2007; Guittet et al, 2007; Levi et al, 2007).
Under identical conditions as in our cell culture experiments (i.e., 37 °C and complete endothelial cell culture medium), Hb heme-iron oxidation with production of HbFe3+ and HbFe4+ was similar for human Hb, αXLHb, bvHb, and the Hb/Hp complex.
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