Phosphorylation of proteoglycans from human articular cartilage by a cAMP-dependent protein kinase.

Abstract

Purified proteoglycan subunits from human articular, bovine articular and nasal cartilages, and a rat chondrosarcoma were phosphorylated in vitro by beef heart cAMP-dependent protein kinase in the presence of gamma 32P-ATP. In these experiments, a maximum of 1.7 moles of 32P were incorporated per mole of proteoglycan from human cartilage. Phosphorylation… (More)

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@article{Anderson1984PhosphorylationOP, title={Phosphorylation of proteoglycans from human articular cartilage by a cAMP-dependent protein kinase.}, author={Roger S. Anderson and Edith R. Schwartz}, journal={Arthritis and rheumatism}, year={1984}, volume={27 9}, pages={1023-7} }