Abstract
AbstractA high-molecular-weight aspartyl proteinase complex, sensitive to pepstatin A was purified to near electrophoretic homogeneity from dry seeds ofjack pine (Pinus banksiana, Lamb.). Two partial activities, endo-and exo-proteinolytic, were associated with the complex, judged by the analysis of haemoglobin hydrolysis products. The high activity of this enzyme in dry jack pine seed suggests a possible function in early germination.
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.
