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.

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

Comparative evaluation of plasma protein purification and 2-D gel electrophoresis protocols for analysis of HIV-1 infected plasma proteins (Preprint)

2021 ◽  
Author(s):  
Mr Sushanta Kumar Barik Sr ◽  
Deepika Varshney ◽  
Deepa Bisht Sr ◽  
Shripad A Patil Sr ◽  
Rananjaya Singh Sr ◽  
...  
Keyword(s):  
Protein Purification ◽  
Human Plasma ◽  
Plasma Protein ◽  
Gel Electrophoresis ◽  
Comparative Evaluation ◽  
Plasma Proteins ◽  
Human Plasma Protein ◽  
Sds Page ◽  
Hiv 1 ◽  
Abundance Proteins

BACKGROUND The focus of the study was the comparative evaluation of HIV-1 infected plasma protein purification and 2-D gel electrophoresis protocols. OBJECTIVE Human plasma protein purification is a risk task to perform 2-D gel electrophoresis. Human plasma proteins contain nearly 70% albumin and globulin. The removal of such high abundance high molecular weight proteins is very difficult to perform 2-D gel electrophoresis METHODS To the best of our knowledge, we searched several research papers, developed and adopted various organic and non-organic based protocols for HIV-1 infected human plasma protein purification and various isoelectrofocusing protocols in 2-D gel electrophoresis RESULTS After failure in 2-D gel-electrophoresis performance by these protocols, Aurum serum mini kit (Bio-Rad, USA) was adopted for plasma protein purification for performing 2-D gel electrophoresis. The low-abundance proteins were better resolved by 10% SDS-PAGE in 2-D gel-electrophoresis. Then, we extended the MALDI-TOF/TOF analysis of low-abundance proteins in human plasma by adopting the Aurum serum mini kit ( Bio-Rad, USA) for 2-D gel electrophoresis. CONCLUSIONS Thus, we concluded that, the Aurum serum mini kit (Bio-Rad, USA) is best to perform the 2-D gel electrophoresis of HIV-1 infected human plasma by depleting the high abundant proteins like albumin and globulin

Species differences in drug plasma protein binding

MedChemComm ◽  
2014 ◽  
Vol 5 (7) ◽  
pp. 963-967 ◽  
Author(s):  
Nicola Colclough ◽  
Linette Ruston ◽  
J. Matthew Wood ◽  
Philip A. MacFaul
Keyword(s):  
Drug Discovery ◽  
Protein Binding ◽  
Human Plasma ◽  
Plasma Protein Binding ◽  
Plasma Protein ◽  
Plasma Proteins ◽  
Species Differences ◽  
Human Plasma Protein ◽  
Binding Data ◽  
Drug Plasma

Comparison of the human plasma protein binding data for a variety of drug discovery compounds indicates that compounds tend to be slightly more bound to human plasma proteins, than compared to plasma proteins from rats, dogs or mice.

Endogenous Heparin Activity In Normal Human Plasma

1981 ◽  
Author(s):  
Hyman Engelberg ◽  
Stephen Lee
Keyword(s):  
Human Plasma ◽  
Plasma Proteins ◽  
Scientific Literature ◽  
Factor Xa ◽  
Activated Partial Thromboplastin Time ◽  
Chromogenic Substrate ◽  
Normal Human Plasma ◽  
Heparin Activity ◽  
Normal Human ◽  
Time Test

The scientific literature is contradictory as to the normal presence of heparin activity in human blood. The question has physiologic and clinical significance. The purpose of this study was to investigate whether biologic heparin activity was demonstrable in extracts of normal human plasma. The method involved initial precipitation of the plasma proteins by methanol-acetone, proteolysis of the precipitated proteins by papase or trypsin, dialysis of the supernatant, lyophilization, and then assay. The final extract showed heparin activity using the Kabi chromogenic substrate, the activated partial thromboplastin time test, and the anti factor Xa procedure. The level of heparin activity was 10-25 units % (app. 1-2 mg/L of plasma). We conclude that endogenous heparin activity is present in normal human plasma at physiologically significant levels, and that it is protein bound.

Performances of an Artificial Reagent for the One-stage Factor IX Assay

1975 ◽  
Vol 33 (03) ◽  
pp. 547-552 ◽  
Author(s):  
L Meunier ◽  
J. P Allain ◽  
D Frommel
Keyword(s):  
Human Plasma ◽  
Factor Ix ◽  
Severe Haemophilia ◽  
Normal Human Plasma ◽  
Haemophilia B ◽  
One Stage ◽  
Normal Human ◽  
The One

SummaryA mixture of adsorbed normal human plasma and chicken plasma was prepared as reagent for factor IX measurement using a one-stage method. The substrate was found to be specific for factor IX. Its performances tested on samples displaying factor IX activity ranging from <l%–2,500% compared favorably with those obtained when using the plasma of severe haemophilia B patients as substrate.

Analysis of Intrinsic Fibrinolysis in Human Plasma Induced by Dextran Sulfate

1992 ◽  
Vol 67 (04) ◽  
pp. 440-444 ◽  
Author(s):  
Hiroko Tsuda ◽  
Toshiyuki Miyata ◽  
Sadaaki Iwanaga ◽  
Tetsuro Yamamoto
Keyword(s):  
Molecular Weight ◽  
Human Plasma ◽  
Dextran Sulfate ◽  
Tissue Type ◽  
Factor Xii ◽  
Normal Human Plasma ◽  
High Molecular Weight Kininogen ◽  
Single Chain ◽  
Major Pathway ◽  
Normal Human

SummaryThe analysis of normal human plasma by fibrin autography revealed four species of plasminogen activator (PA) activity related to tissue-type PA, factor XII, prekallikrein and urokinase-type PA (u-PA). The u-PA activity increased significantly by incubating plasma with dextran sulfate. This increase was coincident with both the cleavage of factor XII and the complex formation of activated factor XII with its plasma inhibitors, which were determined by immunoblotting procedure. The dextran sulfate-dependent activation of u-PA required both factor XII and prekallikrein, but did not require either plasminogen or factor XI. High molecular weight kininogen was required only at a low concentration of dextran sulfate. Thus the results indicate that the factor XII and prekallikrein-mediated activation of single chain u-PA (scu-PA) operates as a major pathway of scu-PA activation in whole plasma in contact with dextran sulfate.

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