Abstract:
:A high affinity cAMP-binding protein (cABP II) was purified to homogeneity from wheat germ. The apparent molecular weight of cABP II, as determined from gel exclusion chromatography, is 5.2 x 10(5) (at low ionic strength) and 2.8 x 10(5) (at high ionic strength). One polypeptide subunit (molecular weight, 80,000) was resolved by polyacrylamide gel electrophoresis of cABP II under subunit dissociating conditions. The purification protocol employed resolves cABP II from a distinct, less acidic cAMP-binding protein (cABP I). The K(d) values for cAMP are about 10(-6) molar and 10(-7) molar for cABP II and cABP I, respectively. The cAMP-binding sites of cABP I and cABP II have a marked adenine-analog specificity, binding adenine, adenosine, adenine-derived nucleosides and nucleotides and a variety of adenine derivatives having cytokinin activity. While cABP II is phosphorylated in reactions catalyzed by endogenous protein kinases, there is no evidence for modulation of these cABP II-protein kinase interactions by cAMP.
journal_name
Plant Physioljournal_title
Plant physiologyauthors
Polya GM,Bowman JAdoi
10.1104/pp.68.3.577subject
Has Abstractpub_date
1981-09-01 00:00:00pages
577-84issue
3eissn
0032-0889issn
1532-2548journal_volume
68pub_type
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