Bovine Platelet Proteins

1969 ◽  
Vol 21 (03) ◽  
pp. 409-418 ◽  
Author(s):  
S Łopaciuk ◽  
N. O Solum
Keyword(s):  
Bovine Serum ◽  
Protein Composition ◽  
Disc Electrophoresis ◽  
Plasma Fibrinogen ◽  
Plasma Albumin ◽  
Precipitin Line ◽  
Bovine Plasma ◽  
Platelet Proteins

Summary1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

Bovine Platelet Proteins III. Some Properties of Platelet Fibrinogen

1969 ◽  
Vol 21 (03) ◽  
pp. 428-440 ◽  
Author(s):  
N. O Solum ◽  
S Łopaciuk
Keyword(s):  
Intrinsic Viscosity ◽  
Rabbit Antiserum ◽  
Disc Electrophoresis ◽  
Carbohydrate Content ◽  
Plasma Fibrinogen ◽  
Total Amino Acid ◽  
Electrophoretic Mobilities ◽  
Bovine Plasma ◽  
Starch Gel ◽  
The Difference

Summary1. Some properties of purified bovine platelet fibrinogen have been described and the data compared to those obtained by parallel analysis of purified bovine plasma fibrinogen.2. A close similarity was found between platelet and plasma fibrinogen as to sedimentation coefficients, electrophoretic mobilities in starch gel and polyacrylamide disc electrophoresis, light absorption spectra in the range 240 mμ to 330 mμ, ability to form immunoprecipitate with a rabbit antiserum against bovine plasma fibrinogen, total amino acid composition and in N-terminal amino acids.Differences between the fibrinogens were found as to intrinsic viscosity, carbohydrate content and behaviour upon clotting by thrombin. Intrinsic viscosity in 0.3 M NaCl at 25° was 0.48 dl/g for platelet fibrinogen as compared to 0.26 dl/g for plasma fibrinogen. The carbohydrate content of platelet fibrinogen was 0.56 ± 0.10% 1.56±0.10% and 1.37±0.09% for sialic acid (calculated as N-glycolyl neuraminic acid), hexose (galactose/mannose 1:2) and hexosamine (glucosamine), respectively. These values were 6, 54 and 26% higher than those found for plasma fibrinogen. The difference in clotting behaviour indicated a slower polymerization rate of the fibrin monomers formed from platelet fibrinogen than of those formed from plasma fibrinogen.

Bovine Platelet Proteins II. Purification of Platelet Fibrinogen

1969 ◽  
Vol 21 (03) ◽  
pp. 419-427 ◽  
Author(s):  
N. O Solum ◽  
S Łopaciuk
Keyword(s):  
Analytical Ultracentrifugation ◽  
Insoluble Fraction ◽  
Disc Electrophoresis ◽  
Plasma Fibrinogen ◽  
Starch Gel Electrophoresis ◽  
Freezing And Thawing ◽  
Insoluble Material ◽  
High Resolution Power ◽  
Starch Gel ◽  
Platelet Proteins

Summary1. Platelet fibrinogen has been purified from washed bovine platelets. The procedure was based on the methods for purification of plasma fibrinogen by fractionated precipitations and extractions with ethanol and glycine below 0°, and precipitation of proteins by dimethylformamide at 0°.2. The platelet extract obtained by freezing and thawing of the cells, freed from insoluble material by centrifugation at 23,000 x g for 30 min, contained 0.22 ±0.003mg fibrinogen per 109 platelets. Total protein of this fraction was 0.77 ±0.08 mg per 109 platelets whereas that of the insoluble fraction was 0.79 ±0.09 mg per 109 platelets.3. The most purified platelet fibrinogen fraction contained 91-98% of the protein in a thrombin-clottable state. The yield was approx. 20%. It showed homogeneity in analytical ultracentrifugation, in immunoelectrophoresis using an antiserum produced by immunization of rabbits against platelet extract, and in starch gel electrophoresis using a discontinuous system of Tris HCl and borate buffers offering a high resolution power towards the platelet proteins. Polyacrylamide disc electrophoresis revealed two to three faint lines behind the main fibrinogen line. At least one such line was also observed with purified plasma fibrinogen.

scholarly journals Selective phagocytic paralysis induced by immobilized immune complexes.

1975 ◽  
Vol 142 (4) ◽  
pp. 827-838 ◽  
Author(s):  
M Rabinovitch ◽  
R E Manejias ◽  
V Nussenzweig
Keyword(s):  
Yeast Cell ◽  
Immune Complexes ◽  
Bovine Serum ◽  
Cell Walls ◽  
Fetal Bovine Serum ◽  
Selective Inhibition ◽  
Peritoneal Macrophages ◽  
Plasma Albumin ◽  
Bovine Plasma ◽  
Fetal Bovine

The phagocytic recognition by peritoneal macrophages plated on glass- or plastic-bound immune complexes of bovine plasma albumin (BSA) and anti-BSA was examined. Ingestion but not the attachment of erythrocytes opsonized with an IgG rich antiserum (EA) was markedly inhibited. In contrast, macrophage interactions with complement-coated (EAC) red cells, or ingestion of latex particles, yeast cell walls or glutaraldehyde-treated erythrocytes was not inhibited. Complexes prepared with pepsin-treated anti-BSA IgG were ineffective indicating a requirement for the Fc region. Inhibition of ingestion of EA was not a consequence of macrophage spreading and did not appear to be mediated by solubilized complexes or by cell-derived inhibitors of phagocytosis. Significant restoration of the ability to ingest EA was obtained when macrophages on complex-coated substrates were incubated for 4-8 h in medium enriched with mouse or fetal bovine serum. Restoration was also attained by removing macrophages from complex-coated dishes and replating onto uncoated dishes. The selective inhibition of ingestion of EA may be due to blocking of Fc receptors by the complexes but depletion of receptors by endocytosis of complexes cannot be ruled out. Alternatively, the complexes may have induced selective failure of the interiorization mechanism.

scholarly journals An Endonuclease Associated with Bovine Plasma Albumin Fraction

1972 ◽  
Vol 247 (1) ◽  
pp. 193-198
Author(s):  
Motoaki Anai ◽  
Hiroyuki Haraguchi ◽  
Yasuyuki Takagi
Keyword(s):  
Plasma Albumin ◽  
Albumin Fraction ◽  
Bovine Plasma

The Relation of Free Sulfhydryl Groups to Chromatographic Heterogeneity and Polymerization of Bovine Plasma Albumin*

Biochemistry ◽  
1962 ◽  
Vol 1 (1) ◽  
pp. 60-68 ◽  
Author(s):  
Robert W. Hartley ◽  
Elbert A. Peterson ◽  
Herbert A. Sober
Keyword(s):  
Sulfhydryl Groups ◽  
Plasma Albumin ◽  
Bovine Plasma

CD-resolved secondary structure of bovine plasma albumin in acid-induced isomerization*

2009 ◽  
Vol 22 (3) ◽  
pp. 333-340 ◽  
Author(s):  
SEIICHI ERA ◽  
HIROSHI ASHIDA ◽  
SHUNJI NAGAOKA ◽  
HIROSHI INOUYE ◽  
MASARU SOGAMI
Keyword(s):  
Secondary Structure ◽  
Plasma Albumin ◽  
Bovine Plasma

Effects of smoking and abstention from smoking on fibrinogen synthesis in humans

2001 ◽  
Vol 100 (4) ◽  
pp. 459-465 ◽  
Author(s):  
Kirsty A. HUNTER ◽  
Peter J. GARLICK ◽  
Iain BROOM ◽  
Susan E. ANDERSON ◽  
Margaret A. McNURLAN
Keyword(s):  
Risk Factors ◽  
Significant Risk ◽  
Plasma Fibrinogen ◽  
Fibrinogen Concentration ◽  
Primary Role ◽  
Absolute Rate ◽  
Albumin Synthesis ◽  
Plasma Albumin ◽  
Concomitant Reduction ◽  
Metabolic Mechanism

Cigarette smoking and hyperfibrinogenaemia are both significant risk factors for the development of cardiovascular disease. Two studies are described here which aimed to establish the metabolic mechanism responsible for the raised plasma fibrinogen concentration observed in smokers. Chronic smokers had a significantly elevated absolute rate of fibrinogen synthesis (ASR) compared with non-smokers (22.7±1.3 mg/kg per day versus 16.0±1.3 mg/kg per day; means±S.E.M., P < 0.01), with plasma levels of fibrinogen significantly correlated with fibrinogen synthesis (r = 0.65, P = 0.04). Unlike fibrinogen, plasma albumin concentrations were lower in smokers than in non-smokers (45±0.4 versus 47±0.7 g/l, P < 0.05), but there was no difference in rates of albumin synthesis between the two groups. Two weeks cessation from smoking by previously chronic smokers was associated with a rapid and marked fall in plasma fibrinogen concentration (from 3.06±0.11 g/l to 2.49±0.14 g/l, P < 0.001), and a significant reduction in ASR (a 33% reduction, from 24.1±1.7 to 16.1±1.0 mg/kg per day, P < 0.001). These studies suggest a primary role for increased synthesis in producing the hyperfibrinogenaemia associated with smoking. Moreover, abstention from smoking for a period of only 2 weeks induces a significant decrease in the rate of fibrinogen synthesis by the liver, with a concomitant reduction in the plasma fibrinogen concentration.

The Aggregation of Bovine Plasma Albumin at Low pH1

1960 ◽  
Vol 82 (14) ◽  
pp. 3741-3745 ◽  
Author(s):  
Edward J. Williams ◽  
Joseph F. Foster
Keyword(s):  
Plasma Albumin ◽  
Bovine Plasma
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