Plasma Proteins in Normal Human Urine1

2015 ◽  
pp. 7-19 ◽  
Author(s):  
Ingemar Bergg�rd
Keyword(s):  
Plasma Proteins ◽  
Normal Human

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.

Plasma Protein, Symposia on Nutrition of the Robert Gould Research Foundation

PEDIATRICS ◽  
1951 ◽  
Vol 8 (5) ◽  
pp. 751-752
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Original Research ◽  
Edema Formation ◽  
Disease States ◽  
Serum Fractions ◽  
Normal Human ◽  
Amino Acid Antagonists ◽  
Relationship Of

This volume contains 17 separate papers or chapters reporting results of original research and discussions by recognized authorities on all important aspects of the plasma protein problem. Some of the topics discussed which are of special interest to the clinician are those relating to (1) the fractionation and properties of normal human plasma proteins, (2) plasma protein formation in health and in various disease states, (3) effects of various types of diet on plasma protein fabrication, (4) the fate of intravenously administered human plasma proteins in health, in idiopathic hypoproteinemia and in osteoporosis, (5) the mechanism of edema formation in relationship to hypoproteinemia, (6) the relationship of protein metabolism to resistance to infection, (7) the influence of the adrenal cortex on plasma protein formation and utilization and (8) the quantitative immunochemical data concerning antibody-containing serum fractions obtained by salt precipitation, alcohol precipitation or delipidation. A new approach to certain obscure metabolic disorders may, in the opinion of the reviewer, grow out of studies on amino acid antagonists discussed in the Symposium by one author.

Tritiated Fluorescein Binding to Normal Human Plasma Proteins

1980 ◽  
Vol 98 (9) ◽  
pp. 1643-1645 ◽  
Author(s):  
D. C. Ianacone ◽  
N. T. Felberg ◽  
J. L. Federman
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Normal Human Plasma ◽  
Normal Human

scholarly journals The isolation and identification of the P-component of normal human plasma proteins (Short Communication)

1974 ◽  
Vol 143 (1) ◽  
pp. 253-254.2 ◽  
Author(s):  
Paul Binette ◽  
Margaret Binette ◽  
Evan Calkins
Keyword(s):  
Human Plasma ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Short Communication ◽  
Normal Human Plasma ◽  
Isolation And Identification ◽  
Human Plasma Protein ◽  
Normal Human

A normal human plasma protein called the P-component, which has a reaction of identity with the pentagonal structure found in amyloid-laden organs, has been isolated and identified with a recently characterized protein, the 9.5S α1-glycoprotein.

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