Morphofunctional characteristics of human platelets in the presence of 0.1-5 mM ascorbic acid were studied. The platelet ability to form lamellae and the preservation of granules in platelets in suspension and during adhesion were evaluated. Ascorbic acid in concentrations of 0.1-1 mM induced no visible changes in platelet structure and did not affect their adhesion activity, but suppressed lamella growth and degranulation in adherent platelets in a dose-dependent manner. The maximum preservation of granules was revealed in the presence of 0.5 mM ascorbic acid (55% in 1 h from the moment of adhesion). In the presence of 2-5 mM ascorbic acid, spontaneous activation and degranulation of platelets was observed. Thus, ascorbic acid is capable of both suppressing and stimulating platelet activity. In concentrations of 0.5-1 mM ascorbic acid can be used to stabilize granules in adherent platelets.
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http://dx.doi.org/10.1007/s10517-023-05690-9 | DOI Listing |
J Neurochem
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NHC Key Laboratory of Cell Transplantation, Department of Neurosurgery, The First Affiliated Hospital of Harbin Medical University, Harbin, China.
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January 2025
Hunan Provincial Key Laboratory of Cytochemistry, School of Chemistry and Chemical Engineering, Changsha University of Science and Technology, Changsha, 410114, PR China.
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January 2025
School of Forensic Medicine, China Medical University, No.77 Puhe Road, Shenyang, Liaoning, 110122, China. Electronic address:
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School of Environmental Science and Engineering, Changzhou University, Changzhou, Jiangsu 213164, People's Republic of China. Electronic address:
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View Article and Find Full Text PDFFood Chem
December 2024
Department of Food and Bioproduct Sciences, University of Saskatchewan, Saskatoon S7N 5A8, Saskatchewan, Canada. Electronic address:
A soluble fraction of faba bean protein was conjugated with tannic acid via the free-radical grafting method using a mixture of ascorbic acid and hydrogen peroxide. Surface plasmon resonance showed a strong bonding between them, while the free amino and thiol group measurements indicated tannic acid's bonding with the amino groups and cysteine residues on the proteins. Structural analysis using intrinsic fluorescence and surface hydrophobicity demonstrated tannic acid's interaction with the aromatic and hydrophobic amino acids of the protein.
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