Thromb Haemost 1965; 14(01/02): 001-011
DOI: 10.1055/s-0038-1654849
Originalarbeiten — Original Articles — Travaux Originaux
Schattauer GmbH

Activated Human Hageman Factor (XII)*

R. J Speer
1   J. K. and Susie L. Wadley Research Institute and Baylor University Graduate Research Institute, Dallas, U.S.A
,
Helen Ridgway
1   J. K. and Susie L. Wadley Research Institute and Baylor University Graduate Research Institute, Dallas, U.S.A
,
J. M Hill
1   J. K. and Susie L. Wadley Research Institute and Baylor University Graduate Research Institute, Dallas, U.S.A
› Author Affiliations
Supported in part by USPHS grants AM-02612 and HE-08025.
Further Information

Publication History

Publication Date:
24 July 2018 (online)

Summary

An improved method for the isolation of highly purified active human Hageman factor has been described. An overall recovery of 25% with a purification of 106 has been achieved. Certain of the physical and chemical characteristics of XII have been elucidated. Selective chemical modification of functional groups and a variety of enzymatic assays have been employed in an effort to shed light on the mechanism of action of this procoagulant.

 
  • References

  • Becker E. L. Inactivation of Hageman Factor by DiisopropylfLuorophosphate (DFP). J. Lab. clin. Med. 56: 136 1960;
  • Biggs R, Macfarlane R. G. Human Blood Coagulation. Charles C. Thomas, Publishers; Springfield: 1953
  • Bodansky A. Phosphatase Studies; Determination of Serum Phosphatase, Factors Influencing Accuracy of Determination. J. biol. Chem. 101: 93 1933;
  • Didisheim P. Purification of Hageman Factor. Fed. Proc. 20: 61 1961;
  • Dodgson K. S, Spencer B. Assay of Sulfatases. In: Glick D. ed. Methods of Biochemical Analysis. Vol. IV, 211 Interscience Publishers; New York: 1957
  • Edsall J. T. The Size, Shape and Hydration of Protein Molecules. In: Neurath H, Bailey K. ed. The Proteins. Vol. I, part B, 549 Academic Press; New York: 1953
  • Fraenkel-Conrat H, Harris J. I, Levy A. L. Recent Developments in Techniques for Terminal and Sequence Studies in Peptides and Proteins. In Glick D. ed. Methods of Biochemical Analysis. Vol. II, 359 Interscience. Publishers; New York: 1955
  • Goldberg L. A, Kutenburg A. M. The Colorimetric Determination of Leucine Amino Peptidase in Urine and Serum of Normal Subjects and Patients with Cancer and Other Diseases. Cancer 11: 283 1958;
  • Haanen G, Hommes F, Berraad H, Morselt G. A Case of Hageman-Factor Deficiency and a Method to Purify the Factor. Thrombos. Diathes. haemorrh. (Stuttg) 05: 201 1960;
  • Hardisty R. M, Margolis J. The Role of Hageman Factor in the Initiation of Blood Coagulation. Brit. J. Haemat. 05: 203 1959;
  • Horowitz H. I, Wilcox W. P, Fujimoto M. M. Assay of Plasma Thromboplastin Antecedent (PTA) with Artificially Depleted Normal Plasma. Blood 22: 35 1963;
  • Hughes B. P. A Method for the Estimation of Serum Creatine Kinase and Its Use in Comparing Creatine Kinase and Aldolase Activity in Normal and Pathological Serums. Clin. chim. Acta. 07: 597 1962;
  • Johnson T. A, Backus H. L. Diagnostic Significance of Determinations of Serum Lipase. Arch, intern. Med. 66: 62 1940;
  • Johnston Jr. GL, 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;
  • Karmen A, Wroblewski F, LaDue J. S. Transaminase Activity in Human Blood. J. clin. Invest. 34: 126 1955;
  • King E. J, Armstrong A. B. Convenient Method for Determining Serum and Bile Phosphatase Activity. Can. med. Ass. J. 31: 376 1934;
  • Lewis J. H. Separation and Molecular Weight Estimation of Coagulation and Fibrinolytic Proteins by Sephadex Gel Filtration. Proc. Soc. exp. Biol. (N. Y.) 116: 120 1964;
  • Lewis M. L, Ware A. G. A One-Stage Method for Determination of Accelerator Globulin. Proc. Soc. exp. Biol. (N. Y.) 84: 640 1953;
  • Margolis J. The Effect of Colloidal Silica of Blood Coagulation. Aust. J. exp. Biol. med. Sei. 39: 249 1961;
  • Meyer K, Rapport M. M. Hyaluronidase. In: Nord F. F. ed. Advances in Enzymology. Vol. 13, 199 Interscience Publishers; New York: 1952
  • Moore S, Stein W. H. Chromatography of Amino Acids on Sulfonated Polystyrene Resins. J. biol. Chem. 192: 663 1951;
  • Owren P. A, Aas K. Control of Dicumerol Therapy and Quantitative Determination of Prothrombin and Proconvertin. Scand. J. clin. Invest. 03: 201 1951;
  • Perelta O, Reinhold J. G. Rapid Estimation of Amylase Activity of Serum by Turbidimetry. Clin. Chem. 01: 157 1955;
  • Putnam F. W. The Chemical Modification of Proteins. In: Neurath H, Bailey K. ed. The Proteins. Vol. I, part B, 893 Academic Press; New York: 1953
  • Ratnoff O. D, Colopy J. E. A Familial Hemorrhagic Trait Associated with a Deficiency of a Clot-Pormoting Fraction of Plasma. J. clin. Invest. 34: 602 1955;
  • Ratnoff O. D, Davie E. W. The Purification of Activated Hageman Factor (Activated Factor XII). Biochem. 01: 967 1962;
  • Ratnoff O. D, Davie E. W, Mallett D. L. Studies on the Action of Hageman Factor: Evidence That Activated Hageman Factor in Turn Activates Plasma Thromboplastin Antecedent. J. clin. Invest. 40: 803 1961;
  • Ratnoff O. D, Davie E. W, Mallett D. L. The Current Status of Knowledge about Hageman Factor. Thrombos. Diathes. haemorrh. (Stuttg) 06: 364 (Suppl. 1) 1961;
  • Schachman H. K. Ultracentrifugation, Diffusion, and Viscometry. In: Colowick S. P, Kaplan N. O. ed. Methods in Enzymology. Vol. IV, 32 Academic Press; New York: 1957
  • Schiffman S, Rapaport S. I, Patch M. J. The Identification and Synthesis of Activated Plasma Thromboplastin Component. Blood.. 22. 733 No. 6 1963
  • Schiffman 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;
  • Schlenk F. Co dehydrogenases I and II and Apoenzymes. In: Sumner J. B, Myrback K. ed. The Enzymes. Vol. II, part I, 250 Academic Press; New York: 1951
  • Schoenmakers JGG, Kurstjens R. M, Haanen C, Zilliken F. Purification of Activated Bovine Hageman Factor. Thrombos. Diathes. haemorrh. (Stuttg) 09: 546 1963;
  • Seligson D. ed. Standard Methods of Clinical Chemistry. Vol. 3. Academic Press; New York: 1961
  • Sherry S, Troll W. The Action of Thrombin on Synthetic Substrates. J. biol. Chem. 208: 95 1954;
  • Shinowara G. Y, Jones L. M, Reinhart H. L. The Estimation of Serum Inorganic Phosphate and “Acid” and “Alkaline” Phosphatase Activity. J. biol. Chem. 142: 921 1942;
  • Soulier J. P, Wartelle O, Menache D. Hageman Trait and PTA Deficiency. The Role of Contact of Blood with Glass. Brit. J. Haemat. 05: 121 1959;
  • Tolksdorf S, McCready M. H, McCullagh D. R, Schwenk E. The Turbidimetric Assay of Hyaluronidase. J. Lab. clin. Med. 34: 74 1949;
  • von Kaulla K. N, Schultz R. L. Methods for the Evaluation of Human Fibrinolysis. Amer. J. clin. Path. 29: 104 1958;
  • Whitaker J. R. Determination of Molecular Weights of Proteins by Gel Filtration on Sepha- dex. Anal. Chem. 35: 1950 1963;
  • Yin E. T, Duckert F. Purification of Factor IX or its Precursor: Isolation of a Hageman- PTA Fraction. Thrombos. Diathes. haemorrh. (Stuttg) 06: 215 1961;