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

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..

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: OILSEEDS-; linseed 12S proteins, characterization of; PROTEINS-VEGETABLE
Subjects: 600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 28 Feb 2018 10:51
Last Modified: 28 Feb 2018 10:51
URI: http://ir.cftri.com/id/eprint/6631

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