Record Details

Isolation and characterization of the 10S fraction of poppy seed proteins.

IR@CSIR-CFTRI

View Archive Info
 
 
Field Value
 
Relation http://ir.cftri.com/6590/
 
Title Isolation and characterization of the 10S fraction of poppy seed proteins.
 
Creator Srinivas, H.
Narasinga Rao, M. S.
 
Subject 03 Proteins
01 Oilseeds
 
Description The high mol. wt. protein fraction was isolated to homogeneity by slow dialysis of 1M NaCl extract of poppy seed meal. The S20,w value of the protein was 10.1S and mol. wt. 215 000. The intrinsic viscosity was 3.5 ml/g, suggesting a compact globular structure for the protein. SDS-PAGE gave 6 nonidentical subunits. The protein had an absorption max. at 278 nm and fluorescence emission max. at 325 nm. It was rich in aspartic and glutamic acids, arginine, and methionine. It also contained 1.15% carbohydrate and very little phosphorus (0.01%). The circular dichroism spectrum showed that the secondary structure of 10S protein consisted of mainly beta-structure and aperiodic structure with little alpha-helix. The protein was highly resistant to hydrolysis by proteolytic enzymes.
 
Date 1986
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/6590/1/J.%20Agric.%20Food%20Chem.%201986%2C%2034%2C%20225-229.pdf
Srinivas, H. and Narasinga Rao, M. S. (1986) Isolation and characterization of the 10S fraction of poppy seed proteins. Journal of Agricultural and Food Chemistry, 34 (2). 225-229, 29 ref.. ISSN 0021-8561