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

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...

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Bibliographic Details
Published in:Plant physiology and biochemistry 2014-10, Vol.83, p.77-87
Main Authors: Swathi, Marri, Lokya, Vadthya, Swaroop, Vanka, Mallikarjuna, Nalini, Kannan, Monica, Dutta-Gupta, Aparna, Padmasree, Kollipara
Format: Article
Language:English
Subjects:
Achaea janata
Activity staining
BBI
Biological and medical sciences
Cajanus - embryology
Castor
Electrophoresis, Gel, Two-Dimensional
Fundamental and applied biological sciences. Psychology
Isoinhibitors
MALDI-TOF/TOF
Native Polyacrylamide Gel Electrophoresis
Plant physiology and development
Protease Inhibitors - chemistry
Protease Inhibitors - pharmacology
Seeds - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Two-dimensional (2-D) gel electrophoresis
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Summary: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 (
ISSN:0981-9428
1873-2690
DOI:10.1016/j.plaphy.2014.07.009