Plasma Protein Cold Ethanol Fractionation

SummaryThe kinetic data of two different 99mTc-Sn-pyrophosphate compounds (compound A and B) were evaluated in non-adult rats. Only compound A concentrated in bone. Both compounds dispersed rapidly in the intravascular as well as the extravascular space. The plasma protein bond of both compounds increased with time after injection and impaired both the renal clearance of both compounds and the bone clearance of compound A. The renal clearance of both compounds was somewhat above that of 5 1Cr-EDTA. It is concluded that compound A and B is mainly excreted by glomerular filtration. About one fourth of the glomerular filtrate of compound B is reabsorbed and accumulated by the tubular cells.

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Factors Regulating Plasma Protein Synthesis IV. Influence of Fragments D and E on Plasma Fibrinogen Concentration

Thrombosis and Haemostasis ◽

10.1055/s-0038-1649178 ◽

1974 ◽

Vol 31 (03) ◽

pp. 395-402 ◽

Cited By ~ 7

Author(s):

V Bocci ◽

T Conti ◽

M Muscettola ◽

A Pacini ◽

G. P Pessina

Keyword(s):

Protein Synthesis ◽

Plasma Protein ◽

Plasma Fibrinogen ◽

Fibrinogen Concentration

SummaryRabbit fibrinogen digest products (FDP) have been separated by Pevikon block electrophoresis yielding fragments D, E and other unidentified FDP.The fragments were injected into rabbits. Surprisingly, as little as 4.3 mg of fragment D elicited a significant increase in plasma fibrinogen concentration 24 hr after injection. The stimulating activity of fragment D is at least 10-fold higher than that of fragment E.

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Purification of Antihemophilic Factor (Factor VIII) by Amino Acid Precipitation*

Thrombosis and Haemostasis ◽

10.1055/s-0038-1654806 ◽

1964 ◽

Vol 11 (01) ◽

pp. 064-074 ◽

Cited By ~ 24

Author(s):

Robert H Wagner ◽

William D McLester ◽

Marion Smith ◽

K. M Brinkhous

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Factor Viii ◽

Plasma Protein ◽

Acid Precipitation ◽

Aminobutyric Acid ◽

Gamma Aminobutyric Acid ◽

Specific Procedure ◽

Beta Alanine ◽

Antihemophilic Factor

Summary1. The use of several amino acids, glycine, alpha-aminobutyric acid, alanine, beta-alanine, and gamma-aminobutyric acid, as plasma protein precipitants is described.2. A specific procedure is detailed for the preparation of canine antihemophilic factor (AHF, Factor VIII) in which glycine, beta-alanine, and gammaaminobutyric acid serve as the protein precipitants.3. Preliminary results are reported for the precipitation of bovine and human AHF with amino acids.

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Functional Relationship of Polymerization Sites of Vertebrate Fibrinogens

10.1055/s-0038-1665661 ◽

1979 ◽

Author(s):

C Cierniewski ◽

T Krajewski ◽

E Janiak

Keyword(s):

Gel Electrophoresis ◽

Functional Relationship ◽

Polyacrylamide Gel Electrophoresis ◽

Polyacrylamide Gel ◽

Functional Similarity ◽

Fractionation Method ◽

Relationship Of ◽

Fibrin Monomers ◽

Fibrinogen Molecule ◽

Cold Ethanol Fractionation

Various studies on the interaction of immobilized mammalian fibrinogen and fibrin monomers with some fibrinogen derivatives demonstrated the presence of two sets of polymerization sites in the mammalian fibrinogen molecule. We obtained the same results while investigating the fibrinogen molecules of other classes of vertebrates /Pisces. Amphibia. Aves/. Despite significant differences among their subunit structures, all of them contain polymerization sites homologous to mammalian counterparts. Moreover, due to great functional similarity, fibrinogen or fibrin monomers of the analyzed species of Pisces. Amphibia. Aves and Mammalia interacted in a specific way with immobilized pig fibrin monomers or fibrinogen, respectively. Using these pig affinity adsorbents, fibrinogen and fibrin monomers of different vertebrates were isolated directly from plasma and analyzed by SDS polyacrylamide gel electrophoresis. Polypeptide compositions of eluted proteins were identical to those obtained for corresponding fibrinogen preparations isolated by cold-ethanol fractionation method. It appears to indicate that the nature of polymerization sites in vertebrate fibrinogens is alike.

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High Levels of Plasma Protein C in Nephrotic Syndrome

Thrombosis and Haemostasis ◽

10.1055/s-0038-1661225 ◽

1985 ◽

Vol 53 (01) ◽

pp. 005-007 ◽

Cited By ~ 16

Author(s):

I Pabinger-Fasching ◽

K Lechner ◽

H Niessner ◽

P Schmidt ◽

E Balzar ◽

...

Keyword(s):

Nephrotic Syndrome ◽

Plasma Protein ◽

Protein C ◽

Inverse Correlation ◽

Elevated Plasma ◽

Significant Inverse Correlation ◽

At Iii ◽

Thrombotic Tendency ◽

Protein C Activity

SummaryIn patients with severe nephrotic syndrome determinations of plasma protein C : Ag levels (8 patients: 5 adults, 3 children) and protein C activity (3 out of 8 patients) revealed significantly elevated plasma protein C concentrations. Furthermore we observed a significant inverse correlation of protein C : Ag to AT III : Ag levels. No protein C : Ag could be detected in the urine of two patients studied. We conclude from our data, that changes of plasma protein C do not contribute to the high thrombotic tendency in nephrotic syndrome.

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