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Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)

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Relation http://oar.icrisat.org/8676/
http://dx.doi.org/10.1016/j.plaphy.2014.07.009
 
Title Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118)
 
Creator Swathi, M
Lokya, V
Swaroop, V
Mallikarjuna, N
Kannan, M
Dutta-Gupta, A
Padmasree, K
 
Subject Pigeonpea
 
Description Proteinase inhibitors (C11PI) from mature dry seeds of Cajanus cajan (cv. ICP 7118) were purified by chromatography which resulted in 87-fold purification and 7.9% yield. SDS-PAGE, matrix assisted laser desorption ionization time-of-flight (MALDI-TOF/TOF) mass spectrum and two-dimensional (2-D) gel electrophoresis together resolved that C11PI possessed molecular mass of 8385.682 Da and existed as isoinhibitors. However, several of these isoinhibitors exhibited self association tendency to form small oligomers. All the isoinhibitors resolved in Native-PAGE and 2-D gel electrophoresis showed inhibitory activity against bovine pancreatic trypsin and chymotrypsin as well as Achaea janata midgut trypsin-like proteases (AjPs), a devastating pest of castor plant. Partial sequences of isoinhibitor (pI 6.0) obtained from MALDI-TOF/TOF analysis and N-terminal sequencing showed 100% homology to Bowman-Birk Inhibitors (BBIs) of leguminous plants. C11PI showed non-competitive inhibition against trypsin and chymotrypsin. A marginal loss (
 
Publisher Elsevier
 
Date 2014
 
Type Article
PeerReviewed
 
Format application/pdf
 
Language en
 
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Identifier http://oar.icrisat.org/8676/1/Plant%20Physiology%20and%20Biochemistry_83_77-87_2014.pdf
Swathi, M and Lokya, V and Swaroop, V and Mallikarjuna, N and Kannan, M and Dutta-Gupta, A and Padmasree, K (2014) Structural and functional characterization of proteinase inhibitors from seeds of Cajanus cajan (cv. ICP 7118). Plant Physiology and Biochemistry, 83. pp. 77-87. ISSN 0981-9428