Regulation of cAMP-dependent protein kinase activity: molecular biological analysis.
نویسندگان
چکیده
منابع مشابه
Regulation of cAMP-dependent protein kinase activity by glutathionylation.
The catalytic subunit of cAMP-dependent protein kinase (cAPK) is susceptible to inactivation by a number of thiol-modifying reagents. Inactivation occurs through modification of cysteine 199, which is located near the active site. Because cysteine 199 is reactive at physiological pH, and modification of this site inhibits activity, we hypothesized that cAPK is a likely target for regulation by ...
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we have investigated the effect of theophylline on the kinetics of the catalytic subunit of protein kinase and related factors in lung tissue. the results show that the point of highest concentration of the c subunit of protein kinase which is active in casein phosphorylation is at 3h of incubation time, but in the presence of 100 ilg/ inl and 10µg/ml theophylline, this is shifted to i.s and 2....
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Two different cAMP-binding proteins have been identified in yeast mitochondria by photoaffinity labelling and based on the occurrence of cAMP-binding activity in two different sub-mitochondrial fractions. One protein (Mr 45-46,000) is tightly bound to the inner mitochondrial membrane whereas the other (Mr 42,000) is found in the soluble intermembrane space. With endogenous substrate cAMP-depend...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1989
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)55961-3