Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2

• Published in: The Journal of biological chemistry Vol. 257; no. 6; pp. 3284 - 3290
• Main Authors: Theurkauf, W E, Vallee, R B
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25.03.1982
• Subjects: Animals; Brain - metabolism; Cattle; Cerebral Cortex - metabolism; Cyclic AMP - metabolism; Kinetics; Macromolecular Substances; Microtubule-Associated Proteins; Microtubules - enzymology; Molecular Weight; Nerve Tissue Proteins - metabolism; Protein Binding; protein kinase; Protein Kinases - isolation & purification; Protein Kinases - metabolism; Proteins - isolation & purification; Proteins - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(19)81107-9

Here the authors report on the molecular and kinetic characterization of the MAP 2-bound kinase. The identity of the cAMP-binding species in bovine brain microtubule preparations was determined using the photoaffinity label 8-azido adenosine 3':5'-( super(32)P)monophosphate. Two polypeptides (M sub(r) = 54,000 and 57,000) with properties characteristic of the dephosphorylated and phosphorylated forms of the regulatory subunit of a type II cAMP-dependent protein kinase (R sub(II)) were specifically labeled. Based on this observation and cAMP-binding data, it is concluded that the MAP 2-bound enzyme was a type II cyclic AMP-dependent protein kinase.