Abstract

Summary Bovine adrenal cortex contains an endogenous factor which selectively inhibits a particular class of cyclic nucleotide independent protein kinase activity (G type casein kinase). This previously purified inhibitor (D. JOB et al. , FEBS Lett., 98 , 303–308) was found to contain typical glycosaminoglycan components. Electrophoretic analysis and selective degradation procedures showed that the inhibitor preparation contained two major glycosaminoglycan moieties identified as heparin-like and chondroitin sulfate-like structures. The casein kinase G inhibitory properties appeared to require intact glycosaminoglycan chains. These findings may suggest a potential role of glycosaminoglycans in the modulation of intracellular protein phosphorylation processes by a particular type of messenger independent protein kinase.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.