Subscribe to RSS
Please copy the URL and add it into your RSS Feed Reader.
https://www.thieme-connect.de/rss/thieme/en/10.1055-s-00035024.xml
Thromb Haemost 1981; 45(03): 233-236
DOI: 10.1055/s-0038-1650177
DOI: 10.1055/s-0038-1650177
Original Article
Studies on the Degradation of Fibrinogen by Proteolytic Enzymes from the Larvae of Lanomia achelous (Cramer)
Further Information
Publication History
Received 08 December 1980
Accepted 20 March 1981
Publication Date:
06 July 2018 (online)
Summary
Fibrinogen degradation products formed by the action of purified haemolymph and saliva of a Satumidae caterpillar of the Lonomia genus were studies by immunoelectrophoresis and polyacrylamide/SDS gel electrophoresis.
The pattern of degradation differ form the one described for plasmin, trypsin, brinase and ochrase. The most striking difference being the rapid loss of the a chain in spite of the presence of the protease inhibitor aprotinin, and/or denaturalizing agents such as 8 M Urea and 2% SDS.
-
References
- 1 Arocha-Pinango CL. Fibrinólisis Produdda por Contacto con Orugas. Acta Cient Venenz 1967; 18: 136-139
- 2 Arocha-Piñango CL, Layrisse M. Fibrinolysis Produced by Contact with a Caterpillar. The Lancet 1969; 01: 810-812
- 3 Arocha-Piñango CL, Perales JE, Gorzula SA. Agents Fibrinolíticos Presentes en los Líquidos Biológicos de una Oruga. Acta Cient Venez 1977; 28: 284-289
- 4 Arocha-Piñango CL, Marsh NA, Robinson DA. Fibrinolytic Agent from a Satumid Caterpillar. Partial Purification and Characterization. Thromb Diath Haemorrh 1973; 29: 135-142
- 5 Astrup T, Mullertz S. Fibrin Plate Method for Estimating Fibrinolytic Activity. Arch of Biochem and Biophys 1952; 40: 346-351
- 6 Marsh NA, Arocha-Piñango CL. Evaluation of the Fibrin Plate Method for Estimating Plasminogen Activators. Thromb Diath Haemorrh 1972; 28: 75-88
- 7 Laemmly UK. Cleavage of Structural Proteins During the Assembly of the Head of Bacteriophage T-4. Nature 1970; 227: 680-685
- 8 Weber K, Osborn M. The Reliability of Molecular Weight Determinations by Dodecyl Sulphate-polyacrylamide Gel Electrophoresis. J Biol Chem 1969; 4406-4412
- 9 Mosesson MW, Galanakis DK, Finlayson JS. Comparison of Human Plasma Fibrinogen Subfractions and Early Plasmin Fibrinogen Derivatives. J Biol Chem 1974; 249: 4656-4664
- 10 Mihalyi E, Weinberg RM, Towne DW, Friedman ME. Proteolytic Fragmentation of Fibrinogen. I. Comparison of the Fragmentation of Human and Bovine Fibrinogen by Trypsin or Plasmin. Biochem 1976; 15: 5372-5381
- 11 Budzynski AZ, Marder VJ, Shainoff JR. Structure of Plasmic Degradation Products of Human Fibrinogen. J Biol Chem 1974; 249: 2294-2302
- 12 Marder VJ, Shulman NR. High Molecular Weight Derivatives of Human Fibrinogen Produced by Plasmin. I. Physicochemical and Immunological Characterization. J Biol Chem 1969; 244 (08) 2111-2119
- 13 Marder VJ, Shulman NR. High Molecular Weight Derivatives of Human Fibrinogen Produced by Plasmin. II. Mechanism of their Anticoagulant Activity. J Biol Chem 1969; 244 (08) 2120-2124
- 14 Mills DA. A Molecular Model for the Proteolysis of Human Fibrinogen by Plasmin. Biochem Biophys Acta 1972; 263: 619-630
- 15 Sanchez-Avalos J, Miller SP. Degradation of Fibrinogen by Proteolytic Enzymes. I. Characterization and Isolation of Products and their Relation to Fibrinolytic States. Thromb Diath Haemorrh 1968; 499-515
- 16 Marder VJ, Budzynski AZ. Date for Defining Fibrinogen and its Plasmic Degradation Products. Thromb Diath Hemorrh 1975; 33: 199-207
- 17 Pizzo SV, Schwartz ML, Hill RL, McKee PA. The Effect of Plasmin on the Subunit Structure of Human Fibrin. J Biol Chem 1973; 248: 4574-4583
- 18 Mosesson MW, Finlayson JS, Galanakis DK. The Essential Covalent Structure of Human Fibrinogen Evidenced by Analysis of Derivatives Formed during Plasmic Hydrolysis. J Biol Chem 1973; 248: 7913-7929
- 19 Mihalyi E, Godfrey JE. Digestion of Fibrinogen by trypsin. I. Kinetic Studies of the Reaction. Biochem Biophys Acta 1963; 67: 73-89
- 20 Mihalyi E, Godfrey JE. Digestion of Fibrinogen by Trypsin. II. Characterization of the Large Fragment obtained. Biochem Biophys Acta 1963; 67: 90-103
- 21 Gaffney PJ, Lord K, Thornes RD. The action of brinase in vitro and in vivo. Thromb Diath Haemorrh 1975; 34: 914 (abst)
- 22 Gormsen J, Feddersen C. Degradation of non-cross linked and cross-linked fibrin clots by plasmin on, trypsin, chymotrypsin and brinase. Thromb Res, 1974; 05: 125-139
- 23 Gaffney PJ. Fibrinolysis by plasmin and brinase. In vitro and in vivoobservations. Progress in Chemical Fibrinolysis and Thrombolysis, Vol 3 1978 Davidson JF, Rowan RM, Samama MM, Desnoyers PC. Raven Press; New York: p 349-372
- 24 Teisseyre E, Latallo ZS, Kopec M. Studies on the proteolysis of fibrinogen and fibrin by Aspergillus ochraceus enzyme as compare to the action of plasmin. Folia Hematológica, (Leipz) 1974; 101: 99-110
- 25 Gaffney PJ, Dobos P. A structural aspect of human fibrinogen suggested by its plasmin degradation. Febbs Lett 1971; 15: 13-16
- 26 Kafatos FC, Tartakoff AM, Law JH, Cacoonase I. Preliminary Characterization of a Proteolytic Enzyme from Silk Months. J Biol Chem 1967; 242 (07) 1477-1487
- 27 Kafatos FC, Tartakoff AM, Cacoonase II. II Substrate Specificity Inhibitors and Classification of the Enzymes. J Biol Chem 1967; 242 (07) 1488-1494
- 28 Katzenellenbogen BS, Kafatos FC. Proteinases of Silk Moth Moulting Fluid Physical and Catalytic Properties. J Insect Physiol 1977; 17: 775-800
- 29 Katzenellenbogen BS, Kafatos FC. Inactive Proteinases in Silk Moth Moulting Gel. J Insect Physiol 1971; 17: 832
- 30 Katzenellenbogen BS, Kafatos FC. General Sterases of Silk Moth Moulting Fluid Preliminary Characterization. J Insect Physiol 1971; 17: 1139-1151
- 31 Jany KD, Haug H, Pfleiderer G, Ishay J. Enzymatic and chemical properties of an endopeptidase from the larva of the hornet Vespa crabro. Biochemistry 1978; 78: 4675-4682
- 32 Yeates RA. Proteinases of female Aedes aegypti (L). Acta Tropica 1978; 35: 195-196
- 33 García ES, Guimaraes JA, Prado JL. Purification and Characterization of a Sulphydryl-Dependent Protease from Rhodnius Prolixus midget. Arch Biochem Biophys 1978; 188: 315-322