PDF herunterladen
Thromb Haemost 1968; 19(03/04): 483-491
DOI: 10.1055/s-0038-1651227
Originalarbeiten – Original Articles – Travaux Originaux
Schattauer GmbH

Properties of Microsomal Activator of Profibrinolysin Found in Bovine and Porcine Heart Muscle

M Nakahara
1   Department of Biochemistry, College of Osteopathic Medicine and Surgery, Des Moines, Iowa, U. S. A.
,
D. R Celander
1   Department of Biochemistry, College of Osteopathic Medicine and Surgery, Des Moines, Iowa, U. S. A.
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Publikationsdatum:
27. Juni 2018 (online)

Auch verfügbar auf
    Lizenzen und Reprints

Summary

Mitochondrial, lysosomal, and microsomal fractions of pig and cow myocardial cells were screened for their ability to effect lysis of bovine fibrin plates prepared with Profibrinolysin-containing and profibrinolysin-free reagents. Little if any activity was observed on profibrinolysin-free fibrin plates. Maximum activity on Profibrinolysin-containing plates was found in association with the microsomes. Extraction of the microsome preparations with 0.15 M KCl and 2.0 M KCl dissolved activator molecules with different pH solubility and stability characteristics. The activator activity of the 2.0 M KCl extract was in general more stable to acid pH than that of the 0.15 M KCl extract.

The activator characteristic of the microsomal suspensions and of both types of microsome extracts was stable to acetone precipitation. However, the 2.0 M KCl extract lost its relatively greater stability to acid pH when precipitated with acetone. The significance of the chemical environment as a determining factor in final properties of purified enzyme molecules is discussed. The importance of using a relatively homogeneous cell population as starting material is also emphasized.

 

  • References

  • 1 Albrechtsen O.K. The fibrinolytic activity of animal tissues.. Acta physiol. scand 1957; 39: 284
    CrossrefPubMedGoogle Scholar
  • 2 Albrechtsen O.K. The fibrinolytic agents in saline extracts of human tissues.. Scand. J. clin. Lab. Invest 1958; 70: 91
    PubMedGoogle Scholar
  • 3 Albrechtsen O.K, Storm O, Classen M. Fibrinolytic activity in some human body fluids.. Scand. J. clin. Lab. Invest 1958; 10: 310
    CrossrefPubMedGoogle Scholar
  • 4 Albrechtsen O.K, Thaysen J.H. Fibrinolytic activity in human saliva.. Acta physiol. scand 1955; 35: 138
    CrossrefPubMedGoogle Scholar
  • 5 Ali S.Y, Lack C.H. Studies on the tissue activator of plasminogen. Distribution of activator and proteolytic activity in the subcellular fractions of rabbit kidney.. Biochem. J 1965; 96: 63
    CrossrefPubMedGoogle Scholar
  • 6 Astrup T. Tissue activators of plasminogen.. Fed. Proc 1966; 25: 42
    PubMedGoogle Scholar
  • 7 Astrup T, Permin P.M. Fibrinolysis in the animal organism.. Nature (Lond.) 1947; 159: 681
    PubMedGoogle Scholar
  • 8 Astrup T, Stage A. Isolation of a soluble fibrinolytic activator from animal tissues.. Nature (Lond.) 1952; 170: 929
    PubMedGoogle Scholar
  • 9 Astrup T, Sterndorjf I. An activator of plasminogen in normal urine.. Proc. Soc. exp. Biol. (N. Y.) 1952; 81: 675
    CrossrefPubMedGoogle Scholar
  • 10 Astrup T, Sterndorff I. A fibrinolytic system in human milk.. Proc. Soc. exp. Biol. (N. Y.) 1953; 84: 605
    CrossrefPubMedGoogle Scholar
  • 11 Astrup T, Sterndorff I. The plasminogen activator in animal tissues.. Acta physiol. scand 1956; 36: 250
    CrossrefPubMedGoogle Scholar
  • 12 Bachmann F, Fletcher A.P, Alkjaersig N, Sherry S. Partial purification and properties of plasminogen activator from pig heart.. Biochemistry 1964; 3: 1578
    CrossrefPubMedGoogle Scholar
  • 13 Celander D.R, Celander E. Characterization of fibrinolytic activity of vascular intima.. Amer. J. Physiol 1966; 211: 319
    PubMedGoogle Scholar
  • 14 Celander D.R, Guest M.M. The biochemistry and physiology of urokinase.. Amer. J. Cardiol 1960; 6: 409
    CrossrefPubMedGoogle Scholar
  • 15 Feamley G.R, Tweed J.M. Evidence of an active fibrinolytic enzyme in plasma of normal people with observations on inhibition associated with the presence of calcium.. Clin. Sci 1953; 12: 81
    PubMedGoogle Scholar
  • 16 Fischer A. Mechanism of the proteolytic activity of malignant tissue cells.. Nature (Lond.) 1946; 157: 442
    PubMedGoogle Scholar
  • 17 Kalckar H.M. Differential spectrophotometry of purine compounds by means of specific enzymes. III. Studies of the enzymes of purine metabolism.. J. biol. Chem 1947; 167: 461
    PubMedGoogle Scholar
  • 18 Kwaan H.C. Tissue fibrinolytic activity studied by a histochemical method.. Fed. Proc 1966; 25: 52
    PubMedGoogle Scholar
  • 19 Lesuk A, Terminiello L, Tarver J.H. Crystalline human urokinase: some properties.. Science 1965; 147: 880
    CrossrefPubMedGoogle Scholar
  • 20 Lewis J.H, Ferguson J.H. Fibrinolysokinase activators for Profibrinolysin.. J. clin. Invest 1950; 29: 1049
    PubMedGoogle Scholar
  • 21 McCall D.C, Kline D.L. Mechanism of action and some properties of a tissue activator of plasminogen.. Thrombos. Diathes. haemorrh. (Stuttg.) 1965; 14: 116
    PubMedGoogle Scholar
  • 22 Mullertz S. A plasminogen activator in spontaneous active human blood.. Proc. Soc. exp. Biol. (N. Y.) 1953; 82: 291
    CrossrefPubMedGoogle Scholar
  • 23 Okamoto V, Takada U. KCl-extracted plasminogen activator in kidney of rabbits.. Keio J. Med 1964; 75: 107
    PubMedGoogle Scholar
  • 24 Shichi H, Sugimura Y, Funahashi S. Haemproteins in heart microsomes. I. Isolation and properties of haemproteolipid.. Biochim. biophys. Acta (Amst.) 1965; 97: 472
    CrossrefPubMedGoogle Scholar
  • 25 Siew C, Gelander D.R. Subcellular localization of bovine endothelial cell activator of the fibrinolytic system.. Physiologist 1966; 9: 286
    PubMedGoogle Scholar
  • 26 Sobel G.W, Mohler S.R, Jones N.W, Dowdy A.B.C, Guest M.M. Urokinase an activator of Profibrinolysin extracted from urine.. Amer. J. Physiol 1952; 171: 678
    PubMedGoogle Scholar
  • 27 Sugiyama Y, Okamoto S. Plasminogen activator in the cytoplasmic granules of rat kidney: Studies on extraction by isotonic and hypertonic salt solutions.. Kobe J. med. Sci 1964; 10: 257
    PubMedGoogle Scholar
  • 28 Tagnon H.J, Petermann M.L. Activation of proplasmin by a tissue fraction.. Proc. Soc. exp. Biol. (N. Y.) 1949; 70: 359
    CrossrefPubMedGoogle Scholar
  • 29 Tiselius A, Hjerten S, Levin D. Protein chromatography on calcium columns.. Arch. Biochem 1956; 65: 132
    CrossrefPubMedGoogle Scholar
  • 30 Todd A.S. Localization of fibrinolytic activity in tissues.. Brit. med. Bull 1964; 20: 210
    CrossrefPubMedGoogle Scholar
  • 31 Vigorito T.F, Celander E, Celander D.R. Origin of urokinase.. Fed. Proc 1965; 24: 512
    PubMedGoogle Scholar
  • 32 Warren B.A. Fibrinolytic properties of vascular endothelium.. Brit. J. exp. Path 1963; 44: 365
    PubMedGoogle Scholar
  • 33 White W.F, Barlow G.H, Mozen M.M. The isolation and characterization of plasminogen activators (urokinase) from human urine.. Biochemistry 1966; 5: 2160
    CrossrefPubMedGoogle Scholar
  • 34 Williams J.R.B. Fibrinolytic activity of urine.. Brit. J. exp. Path 1951; 32: 530
    PubMedGoogle Scholar