Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2
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 polypeptid...
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Published in | The Journal of biological chemistry Vol. 257; no. 6; pp. 3284 - 3290 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
25.03.1982
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Subjects | |
Online Access | Get full text |
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Summary: | 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)81107-9 |