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New biological activity against phospholipase A2 by Turmerin, a protein from Curcuma longa L.
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Mukunda Chethankumar
Published/Copyright:
March 3, 2008
Abstract
Turmerin is a protein from Turmeric (Curcuma longa L.) with a relative molecular mass of 14 kDa. The protein inhibits the enzymatic activity and neutralises the pharmacological properties, such as cytotoxicity, oedema and myotoxicity of multitoxic phospholipase A2 (NV-PLA2) of cobra (Naja naja) venom at a 1:2.5 molar ratio of NV-PLA2:Turmerin. A Lineweaver-Burk plot indicates that Turmerin follows a linear mixed type of inhibition.
Received: 2007-9-4
Accepted: 2007-11-20
Published Online: 2008-03-03
Published in Print: 2008-03-01
©2008 by Walter de Gruyter Berlin New York
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Articles in the same Issue
- Highlight: Oxidative Stress and Senescence
- Regulation of proteasome-mediated protein degradation during oxidative stress and aging
- Cellular responses to reactive oxygen species-induced DNA damage and aging
- Sirt1 protects the heart from aging and stress
- Klotho as a regulator of oxidative stress and senescence
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- Studies on the expression of 6S RNA from E. coli: involvement of regulators important for stress and growth adaptation
- New biological activity against phospholipase A2 by Turmerin, a protein from Curcuma longa L.
- Regulation of the expression of components of the exocytotic machinery of insulin-secreting cells by microRNAs
- Kinetic properties of cathepsin D and BACE 1 indicate the need to search for additional β-secretase candidate(s)
