Genetic Studies of Low-Abundance Human Plasma Proteins IV. Improved Typing of Alpha-1 Acid Glycoprotein (Orosomucoid) by Isoelectric Focusing and Immunoblotting

1987 ◽  
Vol 37 (5) ◽  
pp. 294-299 ◽  
Author(s):  
M.H. Escallon ◽  
R.E. Ferrell ◽  
M.I. Kamboh
Keyword(s):  
Human Plasma ◽  
Isoelectric Focusing ◽  
Plasma Proteins ◽  
Genetic Studies ◽  
Acid Glycoprotein

scholarly journals Sulphation of proteins secreted by a human hepatoma-derived cell line. Sulphation of N-linked oligosaccharides on α2HS-glycoprotein

1986 ◽  
Vol 235 (2) ◽  
pp. 407-414 ◽  
Author(s):  
G Hortin ◽  
E D Green ◽  
J U Baenziger ◽  
A W Strauss
Keyword(s):  
Sialic Acid ◽  
Cell Line ◽  
Human Plasma ◽  
Plasma Proteins ◽  
Human Hepatoma ◽  
Acid Glycoprotein ◽  
Alpha 1 Antitrypsin ◽  
Covalently Linked ◽  
Analytical Approaches ◽  
Endoglycosidase H

Several human glycoproteins, including alpha 1-antitrypsin, alpha 1-acid glycoprotein, transferrin, caeruloplasmin and alpha 2HS-glycoprotein, synthesized by the hepatoma-derived cell line HepG2 were observed to contain covalently linked sulphate. These proteins were estimated to contain about 0.1 mol of sulphate/mol of protein. The most abundant of the sulphated glycoproteins, alpha 2HS-glycoprotein, was analysed in detail. All of the sulphate on this protein was attached to N-linked oligosaccharides which contained sialic acid and resisted release by endoglycosidase H. Several independent analytical approaches established that approx. 10% of the molecules of alpha 2HS-glycoprotein contained sulphate. Our results suggest that a number of human plasma proteins contain small amounts of sulphate linked to oligosaccharides.

Genetic Studies of Low-Abundance Human Plasma Proteins

1989 ◽  
Vol 39 (3) ◽  
pp. 170-173 ◽  
Author(s):  
J.E. Eichner ◽  
M.I. Kamboh ◽  
T. Cook ◽  
R.E. Ferrell
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Genetic Studies

Genetic Studies of Low-Abundance Human Plasma Proteins

1989 ◽  
Vol 6 (2) ◽  
pp. 81-87 ◽  
Author(s):  
L.A. Lyons ◽  
M.I. Kamboh ◽  
R.E. Ferrell
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Genetic Studies

Genetic studies of low-abundance human plasma proteins

1988 ◽  
Vol 81 (1) ◽  
pp. 93-94 ◽  
Author(s):  
M. I. Kamboh ◽  
L. Lyons ◽  
R. E. Ferrell
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Genetic Studies

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.

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