Corn cystatin I expressed in Escherichia coli: investigation of its inhibitory profile and occurrence in corn kernels
1994
M, Abe | Abe, K. | Iwabuchi, K. | Domoto, C. | Arai, S.
Corn cystatin I was expressed in Escherichia coli as a mature protein. It was purified by gel filtration on Sephadex G-50, ion-exchange HPLC, and reversed-phase HPLC. The purified protein showed strong inhibitory activities against papain (Ki: 3.7 X 10(-8) M), and cathepsins H (Ki: 5.7 X 10(-9) M) and L (Ki: 1.7 X 10(-8) M), whereas it inhibited cathepsin B to a lesser extent (Ki: 2.9 X 10(-7) M). Western blot analysis using antibody raised against corn cystatin I revealed that in the corn kernel, the protein occurs with a molecular mass of approximately 13 kDa. Localization in the aleurone layer and embryo of the corn kernel was shown by immunostaining microscopy.
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