Degradación autolítica de la plasmina e isoformas de 5 plasminogenos animales. (Humano, Bovino, Equino, Canino, Ovino de Pelo).

Daniel Iván Barrera V, Amalia Muñoz Gomez, Mauricio Corredor, Luis Fernando Arbeláez R.

Resumen


La principal proteína del sistema fibrinolítico es el plasminógeno, cuyas isoformas nunca han sido analizadas en 2D-PAGE. En este trabajo se han purificado los plasminógenos de cinco especies animales por cromatografía de afinidad (sefarosa- Lisina) caracterizándose posteriormente por electroforesis. En el análisis SDS-PAGE, se ha encontrado una gran similitud en cuanto a la degradación proteolítica del plasminógeno de las cinco especies, no obstante se observa variación en cuanto a las isoformas presentes en los plasminógenos de cada especie por medio del análisis en electroforesis bidimensional.


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Referencias


NILSSON TK, and WALLEN P. (1991) in: Clinical Aspect of Fibrinolysis (Almqvist & Wiksell International, eds. Stockholm)

DOBROVOLSKY AB, and TITAEVA EV. (2002) The fibrinolysis System: Regulation of Activity and Physiologic Functions of Its Main Components. Biochemistry (Moscow), 67, 99-108.

BOOTH NA, ROBBIE LA, CROLL AM, and BENETT AB. (1992) in: The Role of Plasminogen Activators in the Regulation of Connective Tissue Metalloproteinases (Brakman, P & Kluft, C., eds)

COLLEN D. (2001) Role of the Plasminogen System in Fibrin- Haemeostasis and Tissue Remodeling. Haematology, 1-9.

DOOLITTLE RF. (1981) Fibrinogen and Fibrin. Sci. Am. 92-101.

PIZZO S, SCHWARTZ LM, HILL RL, and McKEE P. (1973) The effect of

plasmin on the subunit structure of human fibrin. J. Biol. Chem.1574-83.

FERGUSON EW, FRETTO JL, and McKEE P. (1975) A re-examination of the cleavage of fibrinogen and fibrin by plasmin. J. Biol. Chem. 7210-8.

RÅNBY M. (1982) Studies on Kinetics of Plasminogen Activation by tissue Plasminogen Activator. Biochim. Biophys. Acta 704, 461- 9.

NORRMAN B, WALLEN P, RÅNBY M. (1985) Fibrinolysis mediated by tissue Plasminogen Activator. Disclosure of a Kinetic Transition. Eur. J. Biochem. 149, 193-200.

PAONI NF, and CASTELLINO FJ. (1979) A Comparison of the Urokinase and Streptokinse Activation Properties of the Native and Lower Molecular Weight Forms of Sheep Plasminogen. J. Biol. Chem. 25, 2064-70.

DANO K, ANDREASEN PA, and GRONDHALHANSEN J. (1985) Plasminogen Activators, Tissue Degradation, and Cancer. Adv. Cancer. Res. 44, 139-266

PETERSEN TE, MARTZEN MR, ICHINOSE A, and DAVIE EW. (1990) Characterization of Gene for Human Plasminogen, Key Proenzyme in the Fibrinolytic System. J. Biol.Chem. 265, 6104-11.

SODETZ JM, BROCHWAY WJ, and CASTELLINO FJ. (1972) Multiplicity of Rabbit Plasminogen. Physical Characterization. Biochem. 11, 4441-58.

MAGNUSSON S, and SOTTRUPJENSEN. L. (1976) in: Homologous Kringle Structures Common to Plasminogen and Prothrombin. Substrate Specifity of Enzymes Activating Prothrombin and Plasminogen (Brewk, K &

Ribbons, DW., eds)

LUCAS MA, FRETTO L J, and McKEE PA (1983) The relationsheep of fibrinogen estructure to plasminogen activation and activity plasmina during fibrinolysis. J. Biol. Chem. 258, 4249-4256.

MARKUS G, DEPASCUALE JL, and WISSLER FC. (1978) Quantitative Determination of the binding of eaminocaproic acid to Native Plasminogen. J. Biol. Chem. 253, 727-732.

MOROI M, and AOKI N. (1976) Isolation and Characterization of Plasmin Inhibitor from Human Plasma. J. Biol. Chem. 251, 5956- 5965.

MARTI D, SCHALLER J, OCHENSBERGER B, and RICKLI E. (1994) Expression, purification and characterization of the recombinant

kringle 2 and kringle 3 domains of human plasminogen and analysis of

their binding affinity for - aminocarboxilic acids. Eur. J. Biochem. 219, 455-62.

WALLEN P. (1980) in: Biochemistry of Plasminogen (Klein, DL & Reddy, KNN., eds)

WIMAN B. (1973) Human Plasminogen: Studies on Its Properties and Mechanism of Activation. Umeå University. Medical dissertation No 13.

RÅNBY M. (1982) Studies on Kinetics of Plasminogen Activation by tissue Plasminogen Activator. Biochim. Biophys. Acta 704, 461- 9.

SOTRUPP-JENSEN L. (1978) Amino-Acid sequence of activation cleavage site in Plasminogen: Homology with “pro” part of Prothrombin. Proc.Natl. Acad. Sci. USA, 72, 2577-81. 23.ROBBINS KC. (1995) Dysplasminogenemias. Prog. Card. Dis. 4, 295-308.

AOKI N, MORI M, YOSHIDA N. (1978) Abnormal Plasminogen a Hereditary Molecular Abnormality Found in Patients with Recurrent

Thrombosis. J. Clin. Invest. 61, 1186-95.

RÅNBY M., SUNDELL IB, and NILSSON TK. (1989) Blood Collection in Strong Acidic Citrate Anticoagulant Used in a Study of Dietary Influence on Basal t-PA Activity. Thromb. and Haemost. 62, 917-22.

DEUTSH DG, and MERTZ ET. (1970) Plasminogen: Purification from Human Plasma by Affinity Chromatography. Science 1995-6.

LAEMMLI UK. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-5.

MORRISSEY C. (1981) Silver stain for protein in polyacrylamide gels:

a modified procedure with enhance uniform sensitivity. Anal. Biochem. 117, 307-10.

WIMAN B, and WALLÉN P. (1973) Activation of human Plasminogen

by an insoluble derivative of urokinase. Structural changes of Plasminogen in the course of activation to plasmin and demonstration of a possible

intermediate compound. Europ. J. Biochem. 36, 25-31 .

RICKLI E, and CUENDET PA. (1971) Isolation of plasmin-free human

plasminogen with N-terminal glutamic acid. Biochim. Biophys. Acta 250,447-51

LIU TH, and MERTZ ET. (1970) Studies on Plasminogen. IX. Purification of Human Plasminogen from Cohn Fraction III by Affinity Chromatography. Can. J. Biochem. 49, 1055-61.

SUMMARIA L, ARZADON L, BERNABE P, and ROBBINS KC. (1972) The primary structure of human plasminogen. I. The NH 2 - terminal sequences of human plasminogen and the Scarboxymethyl heavy (A) and light

(B) chain derivatives of plasmin. J. Biol. Chem. 247, 4691- 702.

SUMMARIA L, ARZADON L, BERNABE P, and ROBBINS KC. (1973) Characterization of the NH 2 -terminal glutamic acid and NH 2 -terminal lysine forms of human plasminogen isolated by affinity chromatography and isoelectric focusing methods. J. Biol. Chem. 248, 2984-91.

VIOLAND BN, and CASTELLINO FJ. (1976) Mechanism of the Urokinase-catalized Activation of Human Plasminogen. J. Biol. Chem. 251, 3906-12.

SUMMARIA L, BOREISHA IG, ARZADON L, and ROBBINS K. (1977) Activation of Human Glu- Plasminogen to Glu-Plasmin by Urokinase in Presence of Plasmin Inhibitors. J. Biol. Chem. 252, 3945-51.




DOI: https://doi.org/10.24054/01204211.v2.n2.2004.20

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