The nature of the unhydrolysed fraction of alpha-globulin, the major protein component of Sesamum indicum L. hydrolysed by alpha-chymotrypsin.
Indian J Biochem Biophys
;
1992 Apr; 29(2): 160-7
Article
in English
| IMSEAR
| ID: sea-27564
ABSTRACT
Alpha-globulin, the high molecular weight protein fraction from sesame (Sesamum indicum L.) seed, was hydrolysed by alpha-chymotrypsin. The hydrolysate was resolved into two fractions, the hydrolysed part and the unhydrolysed part of alpha-globulin using gel filtration on Sepharose 6B-100. The unhydrolysed alpha-globulin residue was characterized for its sedimentation coefficient, subunit composition, fluorescence emission spectrum, secondary structure, and other biophysical properties. The results indicated a decrease in the size of the protein molecule upon hydrolysis to a very small extent. The effect of hydrolysis products on hydrolysis of native alpha-globulin as well as on a standard substrate, casein, was also investigated. The results indicated that the hydrolysis products contribute to the resistance of alpha-globulin to proteolysis by alpha-chymotrypsin to the extent of 40%.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Plant Proteins
/
Protein Conformation
/
Seeds
/
Thermodynamics
/
Alpha-Globulins
/
Kinetics
/
Chymotrypsin
/
Amino Acids
/
Hydrolysis
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1992
Type:
Article
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