Abstract
Cyclic nucleotide phosphodiesterase (3′,5′‐cyclic nucleotide nucleotidohydrolase, EC 3.1.4.17) activity isolated from Phaseolus vulgaris L. cv. Limberg seedlings was partially purified and characterized by fractional (NH4)2SO4 precipitation, DEAE‐cellulose chromatography, chromatography on 3′,5′‐cAMP‐agarose, gel permeation chromatography and chromatofocusing. A crude enzyme preparation, a 30–65% (NH4)2SO4 pellet, showed an acidic pH optimum. The enzyme activity was stimulated by imidazole and divalent cations such as Ca2+, Mg2+ and Mn2+, whereas NaF, PPi and Fe3+ were inhibitory. Isobutylmethylxanthine had no significant effect on the plant enzyme. An MI of 42 000 was estimated by gel permeation high performance liquid chromatography. By chromatography on 3′,5′‐cAMP‐agarose a phosphodiesterase was resolved that produced 5′‐AMP as sole reaction product.
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.
