Expanding the Family of Extracellular Chaperones: Identification of Human Plasma Proteins with Chaperone Activity

2021 ◽  
Author(s):  
Nicholas J Geraghty ◽  
Sandeep Satapathy ◽  
Megan Kelly ◽  
Flora Cheng ◽  
Albert Lee ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Chaperone Activity ◽  
The Family

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

Does inbreeding affect N-glycosylation of human plasma proteins?

2011 ◽  
Vol 285 (5) ◽  
pp. 427-432 ◽  
Author(s):  
Ozren Polašek ◽  
Anne-Louise Leutenegger ◽  
Olga Gornik ◽  
Lina Zgaga ◽  
Ivana Kolcic ◽  
...  
Keyword(s):  
Human Plasma ◽  
Plasma Proteins

Binding of calcium by human plasma proteins under simulated physiologic conditions

1964 ◽  
Vol 19 (2) ◽  
pp. 292-296 ◽  
Author(s):  
Irene R. Held ◽  
Smith Freeman
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Protein Concentration ◽  
Calcium Concentration ◽  
Gamma Globulin ◽  
Chloride Concentration ◽  
Total Calcium ◽  
Total Protein Concentration ◽  
Plasma Albumin

The binding of calcium to human plasma albumin, alpha, beta, and gamma globulins was studied with the aid of an ultracentrifuge. The amount of calcium bound to these separated proteins was determined in solutions with electrolyte concentrations and pH within physiological ranges. The total calcium concentration was 2.35–2.90 mm/liter H2O and the total protein concentration was 3.91–4.29 g/100 ml H2O. In these solutions no significant differences were found for the binding of calcium (expressed as mm Ca++ bound per gram protein) by albumin, alpha, and beta globulins; the average values obtained were, respectively, 0.016, 0.018, and 0.023. Significantly less calcium was bound by gamma globulin; 0.009 mm/gram. The pH was varied between 7.200–7.550 and the sodium chloride concentration between 114–157 mEq Na per liter. These changes did not measurably affect the amount of calcium bound to albumin. protein-bound calcium; ultracentrifugation and determination of protein-bound calcium; plasma globulin-bound calcium; plasma albumin-bound calcium Submitted on July 2, 1963

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