Abstract
A lysine-rich serine protease inhibitor, isolated from barley (H. vulgare, var. Hiproly) which inhibits subtilisin strongly, chymotrypsin weaker, but not trypsin, is shown to be homologous with potato inhibitor I (Richardson andCossins, FEBS Lett. 52, 161 (1975)) (45% of the amino acids in identical positions). The barley inhibitor seems to be the first example described of a protease inhibitor from higher plants in which the structure and reactive site is not stabilized by disulfide bonds.
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Abbreviations
- ATEE:
-
acetyltyrosin ethyl ester
- SDS:
-
sodium dodecyl sulfate
- TAME:
-
tosylarginine methyl ester
References
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Svendsen, I., Jonassen, I., Hejgaard, J. et al. Amino acid sequence homology between a serine protease inhibitor from barley and potato inhibitor I. Carlsberg Res. Commun. 45, 389–395 (1980). https://doi.org/10.1007/BF02906163
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DOI: https://doi.org/10.1007/BF02906163