Abstract
A cellulase (β(1:4)4-glucan hydrolase) has been purified 700-fold by cellulose affinity chromatography from anthers of Lathyrus odoratus L. Two forms are present. The major species has a molecular weight of 49 kDa and a p I value of 8.0; the minor a molecular weight of 51 kDa and a p I value of 7.8. Both proteins are recognized by antibodies raised against the ethylene/IAA regulated bean ( Phaseolus vulgaris L.) abscission zone cellulase which has a more basic p I value and some unique antigenic determinants. Ethylene induced Lathyrus flower bud abscission zones contain two forms of cellulase apparently identical to those in the anthers. The possible role of cellulase in the development of anthers is discussed.
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.
