Hydrolysis of polyphosphoinositides by purified sheep seminal vesicle phospholipase C enzymes.

@article{Wilson1984HydrolysisOP,
  title={Hydrolysis of polyphosphoinositides by purified sheep seminal vesicle phospholipase C enzymes.},
  author={David B. Wilson and T E Bross and Sandra Hofmann and Philip W. Majerus},
  journal={The Journal of biological chemistry},
  year={1984},
  volume={259 19},
  pages={11718-24}
}
Sheep seminal vesicles contain two immunologically distinct phospholipase C (PLC) enzymes that can hydrolyze phosphatidylinositol (PI) (Hofmann, S.L., and Majerus, P.W. (1982) J. Biol. Chem. 257, 6461-6469). One of these enzymes (PLC-I) has been purified to homogeneity; the second (PLC-II) has been purified 2600-fold from a crude extract of seminal vesicles. In the present study we have compared the ability of these purified enzymes to hydrolyze PI, phosphatidylinositol 4-phosphate (PI-4-P… CONTINUE READING

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