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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.
M J Swartz, and
H L Mitchell, and
D J Cox, and
G R Reeck
January 1979,
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M J Swartz, and
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G R Reeck
November 1999,
IUBMB life,
M J Swartz, and
H L Mitchell, and
D J Cox, and
G R Reeck
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M J Swartz, and
H L Mitchell, and
D J Cox, and
G R Reeck
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M J Swartz, and
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Biotechnology letters,
M J Swartz, and
H L Mitchell, and
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G R Reeck
January 2007,
Plant physiology and biochemistry : PPB,
M J Swartz, and
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G R Reeck
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M J Swartz, and
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G R Reeck
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M J Swartz, and
H L Mitchell, and
D J Cox, and
G R Reeck
January 1967,
Acta biochimica Polonica,
M J Swartz, and
H L Mitchell, and
D J Cox, and
G R Reeck
November 1980,
Biokhimiia (Moscow, Russia),
