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.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
