A study of the trypsinolysis of pea 11 S globin
1989
Plumb, G.W. | Carr, H.J. | Newby, V.K. | Lambert, N.
The trypsinolysis of hexameric pea 11 S storage globulin (legumin) in high and low ionic strength conditions has been studied in relation to changes observed in subunit composition and quaternary/tertiary structure. Gel filtration, N-terminal analysis and SDS-PAGE revealed details on the probable method of enzyme attack. In high ionic strength a stable intermediate was formed, termed legumin-T. However, in low ionic strength, trypsinolysis proceeded further, completely degrading the tertiary/quaternary structure, with fragmentation to peptides. The site of initial enzyme attack was shown to be at the C-termini of the acidic polypeptides, eventually reducing their molecular mass to 33 0000. The resulting hexameric legumin-t complex was shown by circular dichroism studies to possess a similar secondary structure to that of native legumin. The significance of 11 S globulin proteolysis to structure-function relationships in food systems and its relevance to nutritional value are discussed, together with the application of limited proteolysis for probing structural features of 11 S globulins and proteins in general.
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