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Acitnokinase: A New Natural Therapeutic Molecule for All Types of Thrombosis


Affiliations
1 Division of Microbial Sciences, Agharkar, Research Institute, G. G. Agarkar Road, Pune - 411004, Maharashtra, India
2 Division of Microbial Sciences, Agharkar, Research Institute, G. G. Agarkar Road, Pune - 411004, Maharashtra, India
     

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"A new thermo stable, pH resistant fibrinolytic enzyme was isolated from the cell free spent broth of a Thermophilic Streptomyces Sp. This fibrin-specific, plasminogen-independent molecule exhibits high fibrinolytic activity both in vitro and in vivo studies. It is non-toxic, non-haemolytic, non-allergenic and does not affect red blood cells or other blood proteins. This prokaryotic protein activit ywise resembles urokinase, a eukaryotic protein but structurally it differs as observed from the amino acid sequence of N terminal, the active site. The enzyme most probably diffuses in the blood clot through the light region of the fibrin molecule and attaches the connector rods of the fibrin molecule and then cleaves the fibrin chain randomly."

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  • Acitnokinase: A New Natural Therapeutic Molecule for All Types of Thrombosis

Abstract Views: 204  |  PDF Views: 0

Authors

Sabita Dey
Division of Microbial Sciences, Agharkar, Research Institute, G. G. Agarkar Road, Pune - 411004, Maharashtra, India
Prashanth K. B.
Division of Microbial Sciences, Agharkar, Research Institute, G. G. Agarkar Road, Pune - 411004, Maharashtra, India
Anita Kelkar
Division of Microbial Sciences, Agharkar, Research Institute, G. G. Agarkar Road, Pune - 411004, Maharashtra, India

Abstract


"A new thermo stable, pH resistant fibrinolytic enzyme was isolated from the cell free spent broth of a Thermophilic Streptomyces Sp. This fibrin-specific, plasminogen-independent molecule exhibits high fibrinolytic activity both in vitro and in vivo studies. It is non-toxic, non-haemolytic, non-allergenic and does not affect red blood cells or other blood proteins. This prokaryotic protein activit ywise resembles urokinase, a eukaryotic protein but structurally it differs as observed from the amino acid sequence of N terminal, the active site. The enzyme most probably diffuses in the blood clot through the light region of the fibrin molecule and attaches the connector rods of the fibrin molecule and then cleaves the fibrin chain randomly."

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No Keywords.

References