Fibrinolytic Activity of Two Polypeptide Chains from Human Plasminogen#

Author(s): Agustín Joison*, Gustavo Baiardi, Rocío Donalisio, Federico Gallo.

Journal Name: Current Proteomics

Volume 16 , Issue 4 , 2019

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Graphical 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.

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Article Details

Year: 2019
Page: [277 - 281]
Pages: 5
DOI: 10.2174/1570164616666190112120215
Price: $58

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