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Iron ion induced haemolysis: effect of caeruloplasmin, albumin and ascorbate (vitamin C).
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Human caeruloplasmin (ferroxidase), bovine serum albumin and ascorbate protected washed rat erythrocytes against iron ion stimulated haemolysis, while superoxide dismutase, catalase and other scavengers of "activated oxygen" species had little or no effect. Caeruloplasmin retained its protective
Ascorbate (vitamin C) and dehydroascorbate stimulation of copper induced hemolysis. Protective action of ceruloplasmin, albumin and apotransferrin.
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Copper ion induced lysis of rat erythrocytes was markedly stimulated by low concentrations of ascorbate and dehydroascorbate. Ascorbate oxidase, superoxide dismutase, catalase or scavengers of hydroxyl radicals protected erythrocytes against copper-ascorbate stimulated lysis. It is proposed that
Serum albumin impedes the amyloid aggregation and hemolysis of human islet amyloid polypeptide and alpha synuclein.
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Protein aggregation is a ubiquitous phenomenon underpinning the origins of a range of human diseases. The amyloid aggregation of human islet amyloid polypeptide (IAPP) and alpha synuclein (αS), specifically, is a hallmark of type 2 diabetes (T2D) and Parkinson's disease impacting millions of people
Individualized Correction of the Interference of Hemolysis on Glycated Albumin Determined by the Ketamine Oxidase Method.
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Hemolysis associated with 25% human albumin diluted with sterile water--United States, 1994-1998.
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Since 1994, a shortage of 5% human albumin, a product used off-label during therapeutic plasma exchange (TPE), has existed in the United States. Because of this shortage, hospital pharmacists may prepare 5% solution of human albumin by diluting 25% human albumin with 0.9% NaCl or, when sodium load
[Mechanism of acceleration of acid hemolysis of the E-form of serum albumin].
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The influence of human and bovine serum albumin on the proton-mediated lysis of human, rabbit and sheep erythrocytes was studied. An essential acceleration of hemolysis (2-7-fold) by the action of albumin was observed only at pH values below 4.0, i.e. at values at which the transition of albumin to
Protection by chlorpromazine, albumin and bivalent cations against haemolysis induced by melittin, [Ala-14]melittin and whole bee venom.
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The ability of the peptides melittin, [Ala-14]melittin (P14A) and whole bee venom to lyse red blood cells (RBC) and to cause shape transformation, binding, partitioning and changes in volume of the cells during haemolysis, as well as the action of the bivalent cations Zn2+ and Ca2+, chlorpromazine,
Catecholamine stimulation of copper dependent haemolysis: protective action of superoxide dismutase, catalase, hydroxyl radical scavengers and serum proteins (ceruloplasmin, albumin and apotransferrin).
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Copper induced lysis of washed rat erythrocytes was stimulated by catecholamines, the order of effectiveness being: adrenaline greater than noradrenaline approximately equal to dopamine greater than L-DOPA. The degree of effectiveness is related to the rate of copper ion dependent oxidation of
Hemolysis causes a decrease in HbA1c level but not in glycated albumin or 1,5-anhydroglucitol level.
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HbA1c has been widely used as a glycemic control indicator or as a diagnostic indicator for diabetes mellitus. However, HbA1c is affected by the erythrocyte life span and, therefore, shows falsely low values in hemolytic patients. Erythrocyte creatine (EC) is a sensitive hemolytic marker that
Albumin inhibits hemolysis of erythrocytes induced by ethanolamine oleate during endoscopic injection sclerotherapy.
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In attempts to avoid hemolytic nephropathy following injection of 5% ethanolamine oleate during endoscopic injection sclerotherapy for esophageal varices, the relationship between serum levels of albumin and hemolysis induced by ethanolamine oleate was investigated. The rate of hemolysis at various
Hemolysis of rabbit erythrocytes in the presence of copper ions. Inhibition by albumin and ceruloplasmin.
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The hemolysis of red blood cells (RBC) induced by Cu(II) is modified by ceruloplasmin (Cp) and albumin. The time course of hemolysis for rabbit RBC by Cu(II) consisted of two parts, an induction period followed by a catastrophic lysis period. The induction period decreased and the lysis rate
Trypsin-sensitive, bovine serum albumin-dependent hemolysis activity in Mycoplasma pulmonis.
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Although Mycoplasma pulmonis did not lyse normal erythrocytes, it rapidly lysed erythrocytes that had cytoskeletal deficiencies which allow increased diffusion of membrane glycophorin or that had been treated with trypsin to remove surface proteins. This hemolysis occurred only in the presence of
The cluster [Re6Se8I6]3- induces low hemolysis of human erythrocytes in vitro: protective effect of albumin.
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The cluster Re6Se8I63- has been shown to induce preferential cell death of a hepatic carcinoma cell line, thus becoming a promising anti-cancer drug. Whether this cluster induces acute hemolysis or if it interacts with albumin remains unclear. The effect of acute exposure of human red blood cells to
Fatty acid induced hemolysis. Protective action of ceruloplasmin, albumins, thiols and vitamin C.
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The hemolytic effect of saturated fatty acids increased rapidly, when the number of carbon atoms in the chain exceeded 12. At low fatty acid concentrations (less than 60 microM) the hemolytic effect decreased with increasing number of double bonds in the carbon chain (cis-form fatty acids). A more
Further studies on guinea pig and rabbit cytophilic antibodies directed against human serum albumin. II. In vitro binding properties and the role of cytophilic antibody in plague-formation as measured using the indirect technique of localized hemolysis in gel.
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