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Studies on lipidification of streptokinase: a novel strategy to enhance the stability and activity.
Suthakaran, Pichaimuthu; Balasubramanian, Jaiiamadhumithaa; Ravichandran, Mirunalini; Murugan, Vidhyapriya; Ramya, Lanka Naga; Pulicherla, Krishna Kanth.
Afiliação
  • Suthakaran P; 1Centre for Biotechnology, Anna University, Chennai, India; 2Department of Biotechnology, Acharya Nagarjuna University, Guntur, India; and 3Center for Bioseparation Technology, VIT University, Vellore, India.
Am J Ther ; 21(5): 343-51, 2014.
Article em En | MEDLINE | ID: mdl-24949842
ABSTRACT
Thrombotic disorders and their associated problems are extensively prevalent in developed and developing countries. Streptokinase (SK) is a well-known thrombolytic agent, which is very useful in treating coronary thrombosis and acute myocardial infarction. Several attempts have been made to date to make improvements of this wonderful molecule in terms of reducing or eliminating the problems of eliciting immunogenicity and enhancing the half-life of the molecule. The present research is focused to produce a recombinant SK with enhanced stability and biological activity by the methodology of lipid modification. SK was targeted successfully to the membrane with the help of modified apyrase signal sequence. Higher expression was reported for GJ1158 strain in LBON medium when compared with BL21 (DE3). The obtained recombinant SK was tested for its biological activity by the method of caseinolytic assay. The higher clearance zone was observed in recombinant lipid-modified streptokinase, which denotes the enhanced activity of the protein. The present trial of lipid modification of therapeutics, particularly SK, could help for its superior use as a thrombolytic agent and also paves way for many of the other clinical applications.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Estreptoquinase / Lipídeos Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Estreptoquinase / Lipídeos Idioma: En Ano de publicação: 2014 Tipo de documento: Article