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Cupincin: A Novel Cupin Domain Containing Protease from Rice (Oryza sativa L.) Bran Comprising of Procoagulant and Fibrinogenolytic Activity.

IR@CFTRI: CSIR-Central Food Technological Research Institute, Mysore

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Relation http://ir.cftri.com/13569/
https://dx.doi.org/10.1007/s12288-017-0856-2
 
Title Cupincin: A Novel Cupin Domain Containing Protease from Rice (Oryza sativa L.) Bran Comprising of Procoagulant and Fibrinogenolytic Activity.
 
Creator Sreedhar, R.
Purnima Kaul, Tiku
 
Subject 05 Enzymes
01 Rice
 
Description The current study was carried out to evaluate the pharmacological properties of cupincin- A novel cupin domain containing metalloprotease with limited proteolysis from rice bran on blood coagulation and hydrolysis of human fibrinogen. Cupincin preferentially hydrolyzed the Aa chain of fibrinogen and then the Bb-chain, but not the c-chain. Cupincin reduced the re-calcification time of citrated human plasma dose dependently. Analysis of citrated whole blood in the presence of cupincin by rotem showed a decrease in coagulation time and clot formation time. Sonoclot analysis indicated that cupincin cleaved fibrinogen of whole citrated blood. SDS-PAGE and sonoclot analysis (LI-30) indicated that cupincin lacked plasmin- like activity. Global hemostasis tests like rotem and sonoclot analysis determined cupincin as a procoagulant enzyme. Cupincin did not show any effect on prothrombin time and activated partial thromboplastin time tests suggesting its action on the common pathway of coagulation. The involvement of proteases from rice (Oryza sativa L.) in haemostasis has never been exploited before. This study could provide the basis for the development of new procoagulant agents from a nontoxic source like rice.
 
Date 2018
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/13569/1/Indian%20J%20Hematol%20Blood%20Transfus.pdf
Sreedhar, R. and Purnima Kaul, Tiku (2018) Cupincin: A Novel Cupin Domain Containing Protease from Rice (Oryza sativa L.) Bran Comprising of Procoagulant and Fibrinogenolytic Activity. Indian Journal of Hematology Blood Transfusion, 34 (2). pp. 314-321.