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Thromb Haemost 1971; 25(03): 405-424
DOI: 10.1055/s-0038-1654316
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

Physico-Chemical and Immunological Properties of Bovine Hageman Factor

with the technical assistance of V. F. Schwandt
G. L Grammens
1   Departments of Medicine, Physiology, Pharmacology and Pathology, Wayne Stale University School of Medicine, Detroit, Michigan
2   Department of Medicine, VA Hospital, Allen Park, Michigan
,
A. S Prasad
1   Departments of Medicine, Physiology, Pharmacology and Pathology, Wayne Stale University School of Medicine, Detroit, Michigan
2   Department of Medicine, VA Hospital, Allen Park, Michigan
,
E. F Mammen
1   Departments of Medicine, Physiology, Pharmacology and Pathology, Wayne Stale University School of Medicine, Detroit, Michigan
2   Department of Medicine, VA Hospital, Allen Park, Michigan
,
M. I Barnhart
1   Departments of Medicine, Physiology, Pharmacology and Pathology, Wayne Stale University School of Medicine, Detroit, Michigan
2   Department of Medicine, VA Hospital, Allen Park, Michigan
› Author AffiliationsSupported by U.S.P.H.S. Grant AM-08142 and by a Detroit General Hospital Research Corporation Grant.
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Publication Date:
28 June 2018 (online)

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Summary

By using glass wool absorption followed by elution in strong salt solution and various precipitation methods and DEAE cellulose column chromatography, Hageman factor was purified from bovine plasma. Physico-chemical properties were studied in native protein and in 6 M urea (denatured) which was used in order to prevent monomer - polymer conversion. S°20,w was 7.07 in 0.1 M KC1 and 5.84 in 6 M urea. The intrinsic viscosity by Kragh’s method was 0.0540 ml/g inNaCl-phosphate buffer and 0.0815 ml/g in 6 M urea. Partial specific volume (v) by method based on amino acid residues in undenatured protein, was 0.724 cc/g. By using differential sedimentation equilibrium in 6 M urea-H20 and 6 M urea - D20 solution, v was determined as 0.740 cc/g. In urea, molecular weight (MW) was 142,000 as determined by meniscus depletion method. Similar values were obtained for nondenatured and denatured protein by Sephadex gel filtration, from amino acid composition using Brand’s method and Schachman’s equation. For undenatured and denatured Hageman factor, molar frictional ratios (f/fo) were 1.39 and 1.58, axial ratios were 5.0 and 7.0 and estimation of diffusion constant (D°20, w) based on S-rate, MW and v, gave values of 4.45 x 10-7 and 3.88 x 10-7 cm2/sec respectively. Our data indicate that the molecule was unfolded in 6 M urea solution. Two N-terminal groups, glycine and valine, were demonstrated by Edman procedure. Carbohydrate analysis revealed the following: hexosamine 0.8%, protein- bound hexose 1.9%, fucose 0.19% and sialic acid 0.35%. Isoelectric point was determined as 7.9 by electrofocussing technique. This protein migrated with gamma globulin on electrophoresis. Hageman factor was found to be a powerful immunogen. Anti Hageman factor reacted with both a plasma and a serum protein but not with purified IgG.

 

  • References

  • 1 Ayala W, Moore L. V, Hess E. L. The purple color reaction given by diphenylamine reagent. J. clin. Invest 30: 781 1951;
    CrossrefPubMedSearch in Google Scholar
  • 2 Barnhart M. I. Immunologic technique. In: Thrombosis and Bleeding Disorders. Bang N. U, Beller F. K, Deutsch E, Mammen E. F. Eds. Thieme; Stuttgart: 1970
    Search in Google Scholar
  • 3 Barnhart M. I, Anderson G. F, Baker W. J. Immunochemical studies on proteins important in blood coagulation. Thrombos. Diathes. haemorrh. (Stuttg) 08: 21 1962;
    PubMedSearch in Google Scholar
  • 4 Bencze W. L, Schmid K. Determination of tyrosine and tryptophan in proteins. Anal. Chem 29: 1193 1957;
    CrossrefPubMedSearch in Google Scholar
  • 5 Biggs R, MacFarlane R. G. Human Blood Coagulation. Davis, Philadelphia, Pa. 1962
    Search in Google Scholar
  • 6 Biggs R, Sharp A. A, Margolis J, Hardisty R. M, Stewart J, Davidson W. M. Defects in the early stages of blood coagulation: A report of four cases. Brit. J. Haemat 04: 177 1958;
    CrossrefPubMedSearch in Google Scholar
  • 7 Blombäck B, Blombäck M, Edman P, Hessel B. Human fibrinopeptides : Isolation, characterization and structure. Biochem. biophys. Acta (Amst) 115: 371 1966;
    CrossrefPubMedSearch in Google Scholar
  • 8 Blombäck B, Doolittle R. F. The sequence of amino acids at the N-terminal end of bovine fibrinopeptide B. Acta chem. scand 17: 1816 1963;
    CrossrefPubMedSearch in Google Scholar
  • 9 Blombäck B, Yamashina I. On the N-terminal amino acids in fibrinogen and fibrin. Arkiv Kemi 12: 299 1958;
    PubMedSearch in Google Scholar
  • 10 Blout E. R, Schehter E. A new technique for producing oriented synthetic polypeptide. Biopolymers 01: 565 1963;
    CrossrefPubMedSearch in Google Scholar
  • 11 Boyer S. H. Instructions for starch-gel vertical electrophoresis. Buchler Instruction Manual Fort Lee; N.J: 1964
    Search in Google Scholar
  • 12 Brand E. Amino acid composition of simple proteins. Ann. N.Y. Acad. Sci 47: 187 1946;
    CrossrefPubMedSearch in Google Scholar
  • 13 Cohn E. J, Edsall J. T. Proteins, Amino Acids and Peptides. Reinhold; New York: 1943
    Search in Google Scholar
  • 14 Cohn E. J, Strong L. T, Hughes W. L, Malford D. J, Ashworth J. N, Melin M, Taylor H. L. Preparation and properties of serum and plasma proteins. IV. A system for the separation into fractions of the protein and lipoprotein components of biological tissues and fluids. J. Amer. chem. Soc 68: 459 1946;
    PubMedSearch in Google Scholar
  • 15 Cole E. R, Marciniak E, Seegers W. H. Procedure for the quantitative determination of autoprothrombin C. Thrombos. Diathes. haemorrh. (Stuttg) 08: 434 1962;
    PubMedSearch in Google Scholar
  • 16 Davidson B, Tonney N, Fasman G. D. The optical rotatory dispersion of the ß-structure of poly-L-lysine and poly-L-serine. Biochem. biophys. Res. Commun 23: 156 1966;
    CrossrefPubMedSearch in Google Scholar
  • 17 Didisheim P. Purification of Hageman factor. Fed. Proc 20: 61 1961;
    PubMedSearch in Google Scholar
  • 18 Dische Z, Shettles L. B. A specific color reaction of methylpentoses and a spectrophoto- metric micromethod for their determination. J. biol. Chem 175: 595 1948;
    PubMedSearch in Google Scholar
  • 19 Donaldson V. H, Ratnoff O. D. Hageman factor: Alterations in physical properties during activation. Science 150: 754 1965;
    CrossrefPubMedSearch in Google Scholar
  • 20 Duggan D. E, Udenfriend S. The spectrophotofluorometric determination of tryptophan in plasma and of tryptophan and tyrosine in protein hydrolysates. J. biol. Chem 223: 313 1956;
    PubMedSearch in Google Scholar
  • 21 Edelstein S. J, Schachman H. K. The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J. biol. Chem 242: 306 1967;
    PubMedSearch in Google Scholar
  • 22 Edman P. Method for determination of the amino acid sequence in peptides. Acta chem. scand 04: 283 1950;
    CrossrefPubMedSearch in Google Scholar
  • 23 Edman P. Phenylthiohydantoins in protein analysis. Ann. N.Y. Acad. Sci 88: 602 1960;
    PubMedSearch in Google Scholar
  • 24 Fasman G. Optical rotatory dispersion. In: Methods in Enzymology. Golowick S. P, Kaplan N. O. Eds. Vol. VI. Academic Press; New York: 1957
    Search in Google Scholar
  • 25 Grabar P, Williams G. P. Methode permettant l’etude conjuguee des propriétés electro- phoretiques et immunochimiques d’un melange de proteines. Biochim. biophys. Acta (Amst) 10: 193 1953;
    CrossrefPubMedSearch in Google Scholar
  • 26 Haanen G, Hommes F, Berroad H, Morselt G. A case of Hageman factor deficiency and a method to purify the factor. Thrombos. Diathes. haemorrh. (Stuttg) 05: 201 1960;
    PubMedSearch in Google Scholar
  • 27 Haanen G, Schoenmakers J. G. G. One-stage assay for Hageman factor (Factor XII). Further studies on the role of Hageman factor in blood coagulation. Thrombos. Diathes. haemorrh. (Stuttg) 09: 557 1963;
    PubMedSearch in Google Scholar
  • 28 Haanen G, Morselt G, Schoenmakers J, Maters M, Braams R. The molecular weight of factor XII (Hageman factor) estimated with ionizing radiation. Scand. J. Haemat 02: 248 1965;
    PubMedSearch in Google Scholar
  • 29 Haglund H. Isoelectric focusing in natural pH gradients : A technique of growing importance for fractionation and characterization of proteins. Science Tools 14: 17 1967;
    PubMedSearch in Google Scholar
  • 30 Hunter O. T, Allensworth J. L. Quantitative assay of the Hageman factor. Amer. J. clin. Path 41: 448 1967;
    PubMedSearch in Google Scholar
  • 31 lizuka E, Yang J. T. Optical rotatory dispersion and circular dichroism of the ß form of silk fibroin in solution. Proc. nat. Acad. Sci 55: 1175 1966;
    CrossrefPubMedSearch in Google Scholar
  • 32 Johnson Jr G. L, Ferguson J. H, O’Hanlon F. A. Surface activation of plasma clotting: A function of Hageman factor. Proc. Soc. exp. Biol. (N. Y) 99: 197 1958;
    CrossrefPubMedSearch in Google Scholar
  • 33 Kabat E, Mayer M. Kjeldahl determination: Micro method. In: Experimental Immuno-chemistry. Thomas: Springfield; 111 1948
    Search in Google Scholar
  • 34 Kragh A. M. A Laboratory Manual of Analytical Methods of Protein Chemistry Including Polypeptides. Alexander P, Block R. J. Eds. Pergamon; New York: 1961
    Search in Google Scholar
  • 35 Lundgren H. P, Ward W. H. Molecular size of proteins. In: Amino Acids and Proteins. Greenberg D. M. Ed. Thomas; Springfield: 111 1951.
  • 36 McMeekin T. L, Marshall K. Specific volumes of proteins and the relationship to their amino acid contents. Science 116: 142 1952;
    CrossrefPubMedSearch in Google Scholar
  • 37 Mokrasch L. G. Analysis of hexose phosphates and sugar mixtures with the anthrone reagent. J. biol. Chem 208: 55 1954;
    PubMedSearch in Google Scholar
  • 38 Moore S, Stein W. H. Procedures for the chromatographic determination of amino acids on four per cent cross-linked sulfonated polystyrene resin. J. biol. Chem 211: 893 1954;
    PubMedSearch in Google Scholar
  • 39 Morris G. J. Thin-layer chromatography of proteins on Sephadex G-100 and G-200. J. Chromat 16: 167 1964;
    CrossrefPubMedSearch in Google Scholar
  • 40 Murano G. Some biochemical aspects of the prothrombin complex. Ph. D. dissertation. Wayne State University; Detroit: 1968
    Search in Google Scholar
  • 41 Murano G, Grammens G. L. The amino acid N-terminal sequence analysis. Laboratory Manual. Wayne State University; Detroit: 1967
    Search in Google Scholar
  • 42 Nossel H. L. The contact phase of blood coagulation. Davis, Philadelphia, Penn; 1964
    Search in Google Scholar
  • 43 Ollendorff P. Glass effect and platelet activity in Hageman plasma. Thrombos. Diathes. haemorrh. (Stuttg) 06: 104 1961;
    PubMedSearch in Google Scholar
  • 44 Pedersen K. O. The Ultracentrifuge. Svedberg T, Pedersen K. Eds. Oxford University Press; London and New York: 1940
    Search in Google Scholar
  • 45 Pennel R. B. Fractionation and isolation of purified components by precipitation methods. In: The Plasma Proteins. Putnam F. W. Ed. Vol. I. Academic Press; New York: 1960
    Search in Google Scholar
  • 46 Ratnojf O. D. The biology and pathology of the initial stages of blood coagulation. In: Progress in Hematology. Brown E. B, Moore C. V. Eds. Vol. V. Grune and Stratton; New York and London: 1966
    Search in Google Scholar
  • 47 Ratnoff O. D, Botti R. E, Crum J. D, Donaldson V. H. The activation of PTA (Factor XI) and Hageman factor (Factor XII). Thrombos. Diathes. haemorrh. (Stuttg). Suppl.27; 7 1965
    Search in Google Scholar
  • 48 Ratnojf O. D, Colopy J. Familial hemorrhagic trait associated with a deficiency of a clot- promoting fraction of plasma. J. clin. Invest 34: 602 1955;
    CrossrefPubMedSearch in Google Scholar
  • 49 Ratnojf O. D, Davie E. W. The purification of activated Hageman factor (activated Factor XII). Biochemistry 01: 967 1962;
    CrossrefPubMedSearch in Google Scholar
  • 50 Ratnojf O. D, Rosenblum J. M. Role of Hageman factor in the initiation of clotting by glass ; evidence that glass frees Hageman factor from inhibition. Amer. J. Med 25: 160 1958;
    CrossrefPubMedSearch in Google Scholar
  • 51 Reithel F. J. Dissociation and association of protein structures. Advanc. Protein Chem 18: 124 1963;
    PubMedSearch in Google Scholar
  • 52 Rimington C. Seromucoid and the bound carbohydrate of the serum proteins. Biochem. J 34: 931 1940;
    CrossrefPubMedSearch in Google Scholar
  • 53 Sarkar P. K, Doty P. The optical rotatory properties of the ß-configuration in polypeptides and proteins. Proc. nat. Acad. Sci 55: 981 1966;
    CrossrefPubMedSearch in Google Scholar
  • 54 Seegers W. H, Cole E. R, Aoki N. Functions of Ac-globulin and lipid in blood clotting. Canad. J. Biochem. Physiol 41: 2441 1963;
    PubMedSearch in Google Scholar
  • 55 Seegers W. H, Smith H. P. Factors which influence the activity of purified thrombin. Amer. J. Physiol 137: 348 1942;
    PubMedSearch in Google Scholar
  • 56 Simha R. The influence of Brownian movement on the viscosity of solutions. J. phys. Chem 44: 25 1940;
    CrossrefPubMedSearch in Google Scholar
  • 57 Soulier J. P, Prou-Wartelle O. New data on Hageman factor and plasma thromboplastin antecedent. The role of “contact” in the initial phase of blood coagulation. Brit. J. Haemat 06: 88 1960;
    PubMedSearch in Google Scholar
  • 58 Speer R. J, Ridgeway H, Hill M. J. Activated human Hageman factor (XII). Thrombos. Diathes. haemorrh. (Stuttg) 14: 1 1965;
    PubMedSearch in Google Scholar
  • 59 Speer R, Ridgeway H. The formation and decay of Xlla. Thrombos. Diathes. haemorrh. (Stuttg) 18: 259 1967;
    PubMedSearch in Google Scholar
  • 60 Svedberg T. Mass and size of protein molecules. Nature (Lond) 123: 871 1929;
    CrossrefPubMedSearch in Google Scholar
  • 61 Svedberg T, Pedersen K. O. The Ultracentrifuge. Oxford University Press; London and New York: 1940
    Search in Google Scholar
  • 62 Svennerholm L. Sialic acids and derivatives: Estimation by the ion-exchange method. In: Methods in Enzymology Colowick S. P, Kaplan N. O. Eds. Vol. VI. Academic Press; New York: 1957
    Search in Google Scholar
  • 63 Schachman H. K. Ultracentrifugation, diffusion and viscometry. In: Methods of Enzymology. Colowick S. P, Kaplan N. O. Eds. Vol. IV. Academic Press; New York: 1957
    Search in Google Scholar
  • 64 Schachman H. K, Harrington W. F. Ultracentrifuge studies with a synthetic boundary cell. J. Polymer Sci 12: 379 1954;
    CrossrefPubMedSearch in Google Scholar
  • 65 Schijfman S, Rapaport S. I, Ware A. G, Mehl J. W. Separation of plasma thromboplastin antecedent (PTA) and Hageman factor (HF) from human plasma. Proc. Soc. exp. Biol. (N. Y) 105: 453 1960;
    CrossrefPubMedSearch in Google Scholar
  • 66 Schoenmakers J. G. G, Kurstjens R. M, Haanen C, Zilliken F. Purification of activated bovine Hageman factor. Thrombos. Diathes. haemorrh. (Stuttg) 09: 546 1963;
    PubMedSearch in Google Scholar
  • 67 Schoenmakers J. G. G, Matzke R, Haanen C, Zilliken F. Hageman factor, a novel sialo- glycoprotein with esterase activity. Biochim. biophys. Acta (Amst) 101: 166 1965;
    PubMedSearch in Google Scholar
  • 68 Tombs M. P, Akroyd P. Acrylamide gel electrophoresis. Application No. 18, Shandon Instruments, Sharnbrook, Bedfordshire 1967
    PubMedSearch in Google Scholar
  • 69 Urenes P, Doty P. Optical rotation and the conformation of polypeptides and proteins. In: Advances in Protein Chemistry. Anfinson C, Anson M, Bailey K, Edsall J. Eds. Vol. 16. Academic Press; New York: 1961
    Search in Google Scholar
  • 70 Ware A. G, Guest M. M, Seegers W. H. Fibrinogen : With special reference to its preparation and certain properties of the product. Arch. Biochem 13: 231 1947;
    PubMedSearch in Google Scholar
  • 71 Ware A. G, Seegers W. H. Two-stage procedure for the quantitative determination of prothrombin consumption. Amer. J. clin. Path 19: 471 1949;
    PubMedSearch in Google Scholar
  • 72 Weichselbaum T. E. An accurate and rapid method for the determination of proteins in small amount of blood serum and plasma. Amer. J. clin. Path 16: 40 1946;
    PubMedSearch in Google Scholar
  • 73 Yphantis D. A. Equilibrium ultracentrifugation of dilute solutions. Biochemistry 03: 297 1964;
    CrossrefPubMedSearch in Google Scholar