PubMed · 1962885
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A S de Assis, F V Sobrinho. [Hemospermia].. https://pubmed.ncbi.nlm.nih.gov/1962885/
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Under physiological conditions, red blood cells (RBCs) form aggregates that allow blood flow in all the circulatory system. RBC aggregation is the result of local flow shear stress, erythrocyte properties and macromolecular interactions between adjacent cells. Plasma proteins like fibrinogen or IgG are considered to promote RBC aggregation by a mechanism that remains to be explained. In the present study, we have examined the precise role of IgG on RBC fast-phase aggregation, in comparison with that of fibrinogen. Under our experimental conditions, we observed no fast-phase aggregating effect for IgG, at either physiological or supraphysiological concentrations, while fibrinogen induces strong aggregation of RBC. We also suspect the other plasma proteins to play a role in the RBC aggregating process.
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A new approach to the characterization of biomolecules in whole biological fluids is presented based on simplification of 1H NMR spectra by utilizing differences in molecular diffusion coefficients alone and combinations of relaxation and diffusion parameters. New NMR pulse sequences incorporating both spectral editing features together with solvent water resonance elimination are presented. The methods are exemplified using whole human blood plasma, and it is shown that it is possible to obtain NMR spectra of the slowly diffusing species (generally large molecules) by diffusion editing, the slowly relaxing species (generally small molecules) by spin relaxation editing, or spectra showing any range of molecular mobility using a combination of the two methods. The diffusion-based editing methods are also applicable to the selection of resonances in two-dimensional NMR spectroscopy of biofluids, and we show this for the first time by the production of 1H-1H diffusion-edited TOCSY spectra of human blood plasma where the resonance intensities are weighted according to the molecular diffusion coefficient. In this case, by measuring a diffusion-edited 1H-1H TOCSY NMR spectrum of plasma, it is possible to obtain signals from only the macromolecular components, and this may be of benefit in the analysis of blood lipoproteins. In complex biofluids, the combination of diffusion and relaxation editing brings about considerable spectral simplification leading to an easier resonance assignment process. We also demonstrate the production of 1H NMR spectra with intensities corresponding to diffusion coefficient rather than number of protons, and this opens up new possibilities for pattern recognition classification of samples based on altered molecular mobility features of biofluid components.