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Cited by 335

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Cyclic Nucleotide-dependent Protein Kinases

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Kuo, J.F., Greengard, Paul·1970·Journal of Biological Chemistry

Abstract

Abstract An enzyme which catalyzes the phosphorylation of histone by ATP, and is activated by low concentrations of guanosine 3',5'-monophosphate, has been found in lobster muscle and partially purified. The guanosine 3',5'-monophosphate-dependent protein kinase has been separated from an adenosine 3',5'-monophosphate-dependent protein kinase found in the same tissue. The rate of phosphorylation of histone, catalyzed by the guanosine 3',5'-monophosphate-dependent protein kinase, was increased about 5-fold by guanosine 3',5'-monophosphate at a concentration of 0.5 µm; the apparent Km of the enzyme was about 0.08 µm for guanosine 3',5'-monophosphate and about 4 µm for adenosine 3',5'-monophosphate. The apparent Km of the adenosine 3',5'-monophosphate-dependent protein kinase isolated from the same tissue was about 0.02 µm for adenosine 3',5'-monophosphate and about 1.2 µm for guanosine 3',5'-monophosphate.

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Metadata

Authors
Kuo, J. F., & Greengard, P.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1970-05
Volume
245
Issue
10
Pages
2493-2498
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1650689982
Cited by
335
References
0
FWCI
14.02
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Cyclic Nucleotide-dependent Protein Kinases. https://app.cochat.ai/papers/10.1016/s0021-9258(18)63097-2
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Kuo, J. F., & Greengard, P. (1970). Cyclic Nucleotide-dependent Protein Kinases. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)63097-2

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