JBC, Vol. 252, Issue 22, 8105-8107, Nov, 1977
Isolation and characterization of trypsin inhibitor from opaque-2 corn seeds
M. J. Swartz, H. L. Mitchell, D. J. Cox and G. R. Reeck
Trypsin inhibitor was isolated from seeds of opaque-2 corn by affinity
chromatography on a trypsin/Sepharose column. The two major forms of
inhibitor eluted from the affinity column were separated by DEAE-cellulose
chromatography in the presence of urea. One form of inhibitor is a
single-chain protein that has a molecular weight of approximately 12,500;
the second inhibitor has two polypeptide chains and appears to have been
produced from the single-chain inhibitor by exposure to trypsin in the
affinity chromatography step. The relationship of the inhibitor isolated
from opaque-2 corn to an inhibitor previously isolated from an unspecified
strain of maize by Hochstrasser et al. (Hochstrasser, K., Muss, M., and
Werle, E. (1967) Z. Physiol. Chem. 348, 1337-1340) is discussed.
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