cAMP-dependent protein kinases from the insect Ceratitis capitata

García, José Luis Sánchez; Haro, Amador; Municio, A.M.

doi:10.1016/0003-9861(83)90442-3

Cited by 8 publications

(1 citation statement)

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“…Dissociation of the enzyme into its subunits is not merely a consequence of ion-exchange chromatographies, as is the case of the enzyme from the insect Ceratistis capitata (Garcia et al, 1983). Indeed, when a crude soluble extract from differentiating D. discoideum cells is directly analyzed by gel filtration (not shown) the cAMP-dependent protein kinase is separated into two fractions corresponding to a dimeric RC holoenzyme and to the dissociated subunits, as upon DEAE chromatography (Figure 1).…”

Section: Discussionmentioning

confidence: 99%

An unusual adenosine cyclic 3',5'-phosphate-dependent protein kinase from Dictyostelium discoideum

J¹,

Part²,

Guiso³

et al. 1984

Biochemistry

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The cAMP-dependent protein kinase from Dictyostelium discoideum was extracted from cells at the stage of culmination. Less than 50% of the enzyme remains as a cAMP-dependent holoenzyme in the extracts, and the rest is recovered in the form of dissociated regulatory and catalytic subunits that were purified. The regulatory subunit is a monomeric protein of Mr 42 000 that carries only one cAMP binding site (Xd = 3 nM). The catalytic subunit is also a monomer of M, 40000 with a sedimentation coefficient of 3.3 S. The cAMP-dependent holoenzyme is a dimer consisting

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Section: Discussionmentioning

confidence: 99%