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Isolation and characterization of the major fraction (12 S) of linseed proteins.

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Title Isolation and characterization of the major fraction (12 S) of linseed proteins.
 
Creator Madhusudhan, K. T.
Narendra, Singh.
 
Subject 03 Proteins
01 Oilseeds
 
Description The major protein of linseed, accounting for 66% of the total proteins, was isolated to homogeneity by gel filtration on Sepharose 6B. The protein has an s20,w value of 12 and contained less than 0.5% carbohydrate and no phosphorus. It has an absorption max. at 280 nm and fluorescence emission max. at 320 nm. Circular dichroism studies revealed the protein contained 3% alpha-helix, 17% beta-structure, and the rest aperiodic structure. The 12 S protein showed 5 nonidentical subunits on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) and 6 subunits each on urea-PAGE in acid and alkaline systems. The intrinsic viscosity value was 3.1 ml/g. Mol. wt. estimated by the Archibald method and sedimentation-diffusion measurements was around 294 000. The protein was found to dissociate at acid pH and in low ionic strength buffers.
 
Date 1985
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/6631/1/J.%20Agric.%20Food%20Chem.%201985%2C%2033%2C%20673-677.pdf
Madhusudhan, K. T. and Narendra, Singh. (1985) Isolation and characterization of the major fraction (12 S) of linseed proteins. Journal of Agricultural and Food Chemistry, 33 (4). 673-677, 38 ref..