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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A protein-bound polysaccharide from Basidiomycetes enhances myosin phosphorylation but inhibits myosin ATPase activity: studies with a crude actomyosin preparation of chicken gizzard smooth muscle.

Chicken gizzard actomyosin, containing the calmodulin-myosin light chain kinase (MLCK) system, was incubated in the presence of various concentrations of PSK, a protein-bound polysaccharide from Basidiomycetes, together with Ca2+ and Mg-ATP. The phosphorylation of myosin was enhanced half-maximally by 10-4 g/ml of PSK. However, a similar concentration of PSK reduced the Mg-ATPase activity of the actomyosin. The former was brought about through stimulation of the MLCK activity and the latter through inhibition of the myosin ATPase activity.[1]

References

  1. A protein-bound polysaccharide from Basidiomycetes enhances myosin phosphorylation but inhibits myosin ATPase activity: studies with a crude actomyosin preparation of chicken gizzard smooth muscle. Kaneko, K., Takano-Ohmuro, H., Iwai, T., Kohama, K. J. Biochem. (1991) [Pubmed]
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