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Fibrinolytic Activity of Two Polypeptide Chains from Human Plasminogen#

[ Vol. 16 , Issue. 4 ]

Author(s):

Agustín Joison*, Gustavo Baiardi, Rocío Donalisio and Federico Gallo   Pages 277 - 281 ( 5 )

Abstract:


Background: Plasminogen is a blood plasma glycoprotein of molecular weight about 92,000 Daltons. Physiologically, it incorporates into blood clots and after its activation by plasminogen activators to plasmin can perform a fibrinolytic function. Microplasmin is truncate polypeptide chain derivate of plasmin may be increase the fibrinolytic activity.

Objective: To study the amino acid sequence of two polypeptides chains derivate to the plasminogen with fibrinolytic activity.

Methods: The two polypeptides chains were prepared by isoelectric precipitation of human plasma in sodium borate buffer. The sample in a second step was subjected to affinity and ionic interchange chromatography and denaturalized electrophoresis was carried out on the sample previous heat 70ºC.

Results: Two polypeptide chains of 29.000 and 35.000 Daltons by autolysis controlled were obtained with 25 UI of fibrinolytic activity in fibrin plate.

Conclusion: Microplasmin was obtained with cleavage in different amino acid bounds and rearrangement of amino acids by autolysis with controlled alkaline precipitation.

Keywords:

Plasminogen, plasmin, fibrinolytic activity, fibrin, amino acid sequence, microplasmin.

Affiliation:

School of Chemistry, Catholic University of Cordoba, Cordoba, Institute of Biological and Technological Research (IIBYT-CONICET), National University of Cordoba, School of Chemistry, Catholic University of Cordoba, Cordoba, Institute of Biological and Technological Research (IIBYT-CONICET), National University of Cordoba, School of Chemistry, Catholic University of Cordoba, Cordoba, Institute of Vascular Research, Viedma 493, CP 8332 General Roca, Río Negro

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