scholarly journals Modification of plasma proteins by cigarette smoke as measured by protein carbonyl formation

1992 ◽  
Vol 286 (2) ◽  
pp. 607-611 ◽  
Author(s):  
A Z Reznick ◽  
C E Cross ◽  
M L Hu ◽  
Y J Suzuki ◽  
S Khwaja ◽  
...  
Keyword(s):  
Ascorbic Acid ◽  
Human Plasma ◽  
Gas Phase ◽  
Cigarette Smoke ◽  
Plasma Proteins ◽  
Metal Ion ◽  
Chelating Agents ◽  
Protein Carbonyl ◽  
Plasma Damage ◽  
Carbonyl Formation

Exposure of human plasma to gas-phase (but not to whole) cigarette smoke (CS) produces oxidative damage to lipids [Frei, Forte, Ames & Cross (1991) Biochem. J. 277, 133-138], which is prevented by ascorbic acid. The ability of CS to induce protein damage was measured by the carbonyl assay and by loss of enzyme activity and protein -SH groups. Both whole and gas-phase CS caused formation of carbonyls in human plasma, which was partially inhibited by GSH but not by ascorbic acid or metal-ion-chelating agents. Isolated albumin exposed to CS showed much faster carbonyl formation (per unit protein) than did whole plasma; damage to isolated albumin was partially prevented by chelating agents. Isolated creatine kinase (CK) lost activity upon exposure to CS much faster than did CK in plasma. Direct addition to plasma of mixtures of some or all of the aldehydes reported to be present in CS caused protein carbonyl formation and inactivation of CK, but neither occurred to the extent produced by CS exposure.

scholarly journals Gas phase oxidants of cigarette smoke induce lipid peroxidation and changes in lipoprotein properties in human blood plasma. Protective effects of ascorbic acid

1991 ◽  
Vol 277 (1) ◽  
pp. 133-138 ◽  
Author(s):  
B Frei ◽  
T M Forte ◽  
B N Ames ◽  
C E Cross
Keyword(s):  
Lipid Peroxidation ◽  
Ascorbic Acid ◽  
Blood Plasma ◽  
Gas Phase ◽  
Cigarette Smoke ◽  
Human Blood ◽  
Biological Fluids ◽  
Human Blood Plasma ◽  
Lipid Hydroperoxides ◽  
Protein Thiols

Cigarette smoke (CS) is known to contain a large number of oxidants. In order to assess the oxidative effects of CS on biological fluids, we exposed human blood plasma to filtered (gas phase) and unfiltered (whole) CS, and determined the rate of utilization of endogenous antioxidants in relation to the appearance of lipid hydroperoxides. Lipid peroxidation was measured with a specific and sensitive assay that can detect lipid hydroperoxides at plasma levels as low as 10 nM. We found that exposure of plasma to the gas phase of CS, but not to whole CS, induces lipid peroxidation once endogenous ascorbic acid has been oxidized completely. In addition, CS exposure caused oxidation of plasma protein thiols and albumin-bound bilirubin, whereas uric acid and alpha-tocopherol were not consumed at significant rates. In plasma exposed to the gas phase of CS, low-density lipoprotein exhibited slightly increased electrophoretic mobility, but there was no apparent degradation of apolipoprotein B. Our results support the concept of an increased vitamin C utilization in smokers, and suggest that lipid peroxidation induced by oxidants present in the gas phase of CS leads to potentially atherogenic changes in lipoproteins.

Plasma Components which Interfere with Ristocetin-induced Platelet Aggregation

1975 ◽  
Vol 33 (03) ◽  
pp. 540-546 ◽  
Author(s):  
Robert F Baugh ◽  
James E Brown ◽  
Cecil Hougie
Keyword(s):  
Platelet Aggregation ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Binding Protein ◽  
Plasma Heating ◽  
Protein S ◽  
Fold Increase ◽  
Normal Human Plasma ◽  
Preliminary Examination ◽  
Normal Human

SummaryNormal human plasma contains a component or components which interfere with ristocetin-induced platelet aggregation. Preliminary examination suggests a protein (or proteins) which binds ristocetin and competes more effectively for ristocetin than do the proteins involved in ristocetin-induced platelet aggregation. The presence of this protein in normal human plasma also prevents ristocetin-induced precipitation of plasma proteins at levels of ristocetin necessary to produce platelet aggregation (0.5–2.0 mg/ml). Serum contains an apparent two-fold increase of this component when compared with plasma. Heating serum at 56° for one hour results in an additional 2 to 4 fold increase. The presence of a ristocetin-binding protein in normal human plasma requires that this protein be saturated with ristocetin before ristocetin-induced platelet aggregation will occur. Variations in the ristocetin-binding protein(s) will cause apparent discrepancies in ristocetin-induced platelet aggregation in normal human plasmas.

The binding of the antimalarial arteether to human plasma proteins in-vitro

1992 ◽  
Vol 44 (11) ◽  
pp. 940-942 ◽  
Author(s):  
S. Wanwimolruk ◽  
G. Edwards ◽  
S. A. Ward ◽  
A. M. Breckenridge
Keyword(s):  
Human Plasma ◽  
Plasma Proteins

Human plasma lipid and immunologic responses to eggs and ascorbic acid

1988 ◽  
Vol 8 (4) ◽  
pp. 353-366 ◽  
Author(s):  
Barbara C. O'Brien ◽  
David N. McMurray
Keyword(s):  
Ascorbic Acid ◽  
Human Plasma ◽  
Plasma Lipid
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