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Resistance of alpha-globulin from Sesamum indicum L. to proteases in relationship to its structure.

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Title Resistance of alpha-globulin from Sesamum indicum L. to proteases in relationship to its structure.
 
Creator Tasneem, R.
Prakash, V.
 
Subject 03 Proteins
01 Oilseeds
 
Description alpha-Globulin, the high-molecular-weight protein fraction from Sesamum indicum L., was hydrolyzed to low-molecular-weight protein and peptides by pepsin, while its resistance to hydrolysis by group-specific enzymes, trypsin or alpha-chymotrypsin, was very high. The protein showed definite structural changes after proteolysis, especially after peptic hydrolysis, as evidenced from various biophysical data. The sedimentation velocity pattern of alpha-globulin hydrolyzed by trypsin or alpha-chymotrypsin indicated reduction in the percentage of 11S component, while the pepsin-hydrolyzed sample was devoid of any 11S component, indicating the absence of a native protein molecule. The fluorescence emission spectra of the various hydrolyzed alpha-globulin showed a red shift in the fluorescence emission maximum. The red shift was maximum with alpha-globulin hydrolyzed by pepsin and minimum with the trypsin-hydrolyzed sample. The far-ultraviolet-circular dichroic measurements indicated that most of the ordered structure of alpha-globulin was absent after pepsin hydrolysis, while after trypsin and chymotrypsin hydrolysis conformational changes were less.
 
Date 1989
 
Type Article
PeerReviewed
 
Format pdf
 
Language en
 
Identifier http://ir.cftri.com/2358/1/Journal%20of%20Protein%20Chemistry%2C%20Vol.%208%2C%20No.%202%2C%201989.pdf
Tasneem, R. and Prakash, V. (1989) Resistance of alpha-globulin from Sesamum indicum L. to proteases in relationship to its structure. Journal of Protein Chemistry, 8 (2). pp. 251-61. ISSN 0277-8033