Factor VIII, A series of homologous oligomers and a complex of two proteins
Thrombosis ResearchPublished 1 January 1974
Jan A. van Mourik, Bonno N. Bouma, Wil T. Labruyère, S. de Graaf, I. A. Mochtar
Citations97
SJR quartileQ2
SJR score0.97
SNIP1.03
Generate an AI Snapshot to get a quick, structured summary of this paper.
Study Snapshot
ObjectiveStudy objective
MethodsResearch methodology
PopulationPopulation studied
Sample sizeSample sizes
OutcomesStudy outcomes here
ResultsStudy results comes here
LimitationsResearch study limitations comes here
A concise AI-generated summary of the paper will appear here once you click Generate AI Snapshot.
TL;DR
The results suggest that the intact aggregate is required for factor VIII activity and it is proposed that diminuation of electrostatic repulsion is a factor which contributes to the stability of the aggregates in high ionic strength buffers at neutral pH.
Abstract
Abstract Evidence has been obtained that human antihemophilic factor A behaves as an aggregating series of homologous oligomers. Apparent irreversible dissociation is observed upon dialysis and the extent of dissociation seems to be dependant upon ionic strength and pH of the medium. Dissociation is promoted at low ionic strength at pH 7.0 and results in two components with apparently different precipitating properties on crossed immunoelectrophoresis. It is proposed that diminuation of electrostatic repulsion is a factor which contributes to the stability of the aggregates in high ionic strength buffers at neutral pH. The results further suggest that the intact aggregate is required for factor VIII activity.
Keywords
Materials ScienceMedicine
Archives of Biochemistry and BiophysicsSize and charge isomer separation and estimation of molecular weights of proteins by disc gel electrophoresis
1,902 Citations1968Jerry L. Hedrick, Alan Jay Smith
The molecular weight-slope relation was established utilizing 17 well-characterized proteins as standards and it is possible to determine the molecular weight of a protein with an average precision of ±4%.
Scandinavian Journal of Clinical and Laboratory InvestigationElectroimmuno Assay
1,700 Citations1972C.‐B. Laurell
Analytical BiochemistryA procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis
1,137 Citations1967Andreas Chrambach, R. Reisfeld +2 more
Protein zones may be stained by Coomassie blue without any destaining of the background and with a sensitivity at least as high as that of amido black and at the price of background destaining.
Annals of the New York Academy of SciencesSIMPLIFIED “DISC” (POLYACRYLAMIDE GEL) ELECTROPHORESIS*
569 Citations1964J. T. Clarke
Cross‐linked homogeneous 5 per cent polyacrylamide gel in rod form is a convenient medium for sharp analytical electrophoretic separation in microgram quantities of most serum proteins and of many biological ampholytes.
Clinica Chimica ActaAn improved technique of agar-gel electrophoresis on microscope slides
334 Citations1959R.J. Wieme
A technique of agar-gel electrophoresis possessing a high resolving power is described whereby a minimum of nine fractions are revealed in normal human serum, which seems to be especially promising for the study of tissue proteins and of animal serum proteins.
Journal of Biological ChemistryIsolation and Characterization of Human Factor VIII (Antihemophilic Factor)
215 Citations1973Mark E. Legaz, Gottfried Schmer +2 more
Antibodies to the highly purified human Factor VIII form a precipitin line in immunoelectrophoresis experiments with the cryoprecipitate fraction prepared from hemophilic plasma, indicating that an abnormal Factor VIII molecule is present in the plasma of individuals with classic hemophilia.
Thrombosis and HaemostasisAntihemophilic Factor: Separation of an Active Fragment Following Dissociation by Salts or Detergents
188 Citations1972Whyte G. Owen, Robert H. Wagner
It is proposed that antihemophilic factor activity is associated with a molecule, of relatively low molecular weight, which in plasma or partially purified fractions is bound by electrostatic and hydrophobic bonds to a high molecular weight carrier.
Analytical BiochemistryQuantitative densitometry of 1–50 μg protein in acrylamide gel slabs with coomassie blue
167 Citations1972William N. Fishbein
This pattern suggests that progressive compaction of the protein bands at shorter migration distances is the responsible factor, preventing the stoichiometric uptake of dye molecules once a critical protein concentration has been exceeded.
Nature New BiologyImmunological Characterization of Purified Anti-Haemophilic Factor A (Factor VIII) which corrects Abnormal Platelet Retention in Von Willebrand's Disease
165 Citations1972Barend Bouma, Y. WLEGERINCK +3 more
Normal platelet retention in a column of glass beads, which has been described in cases of Von Willebrand's disease, is corrected in vitro by cryoprecipitate prepared from normal plasma and partially purified factor VIII concentrates although fibrinogen is ineffective.
Thrombosis and HaemostasisDetection of the Carrier State in Hereditary Coagulation Disorders I
146 Citations1968J. J Veltkamp, E. F Drion +1 more
Journal of Clinical InvestigationStudies on the purification and characterization of human factor VIII
108 Citations1972Sally L. Marchesi, N. Raphael Shulman +1 more
The chymotrypsin digestion step facilitates the preparation of factor VIII by reducing the viscosity of fibrinogen in the crude starting material, thereby increasing fivefold the quantity of material which can be processed at one time.
Biochimica et Biophysica Acta (BBA) - Protein StructurePurification of human antihemophilic factor (factor VIII) by gel chromatography
101 Citations1970Jan A. van Mourik, I. A. Mochtar
Journal of Biological ChemistryThe Isolation and Characterization of Bovine Factor VIII (Antihemophilic Factor)
84 Citations1972Gottfried Schmer, Edward P. Kirby +2 more
Bovine Factor VIII (antihemophilic factor) has been purified approximately 10,000-fold with an over-all yield of 10 to 15% and its general properties including its amino acid composition are reported.
Thrombosis and HaemostasisSeparation of Sub-Units of Antihemophilic Factor (AHF) by Agarose Gel Chromatography
75 Citations1972Harvey J. Weiss, Louise Lang Phillips +1 more
These studies provide further evidence that AHF is a high molecular weight substance, not associated with fibrinogen, whose quarternary structure may be disrupted to produce active sub-units of varying sizes.
Journal of Clinical InvestigationStudies on the purification of antihemophilic factor (factor VIII)
73 Citations1969Lawrence Kass, Oscar D. Ratnoff +1 more
Concanavalin A precipitates antihemophilic factor from normal plasma with rapidity, and by combining this precipitation with other techniques, this work was able to separate fractions rich in antihemophile activity from human plasma with rapidlyity.
PubMedIsolation and some chemical properties of human factor VIII (antihemophilic factor).
68 Citations1971Edward J. Hershgold, Audrey M. Davison +1 more
Human factor VIII has been isolated in a highly purified form with the use of an extract of plasma cryoprecipitate as starting material and proves to be a compound protein containing about 76 per cent amino acids, 10 per cent carbohydrates, and 11 per cent of total lipids.
Journal of Biological ChemistryConformational Changes, Inactivation, and Dissociation of Pigeon Liver Fatty Acid Synthetase Complex
59 Citations1972Suriender Kumar, Richard A. Muesing +1 more
It is suggested that hydrophobic forces and a diminution of electrostatic repulsions are factors which contribute to the stability of the complex in high ionic strength buffers at neutral pH.
Analytical BiochemistryPolyacrylamide slab electrophoresis followed by electrophoresis into antibody-containing agarose gel
23 Citations1971Bengt G. Johansson, Johan Stenflo
Archives of Biochemistry and BiophysicsUrease catalysis and structure
18 Citations1972William N. Fishbein, K. Nagarajan
Ionic strength has been found to have an important influence on the polymerization rate of mercaptan-free urease solutions, especially as the solution pH was elevated 1–2 units above the enzyme pI, in qualitative agreement with that predicted by the Debye-Huckel theory.