PMID: 2494377Feb 1, 1989Paper

Are phospholipid-binding proteins in vivo phospholipase inhibitors?

Klinische Wochenschrift
J Poensgen

Abstract

Apo C1, a 6.5 kD protein component of VLDL, inhibits the hydrolysis of DPPC vesicles by pancreatic PLA2 and the hydrolysis of cellular phospholipids by endogenous phospholipases by interaction with the substrate. It is suggested that apo C1 and similar phospholipid-binding proteins modulate in vivo phospholipase activity, because they do so in cell homogenates with concentrations approximately equal to those found in the plasma.

References

Dec 15, 1987·Biochemical Pharmacology·S H PeersR J Flower
Feb 14, 1987·Biochimica Et Biophysica Acta·M Bartolf, R C Franson
Sep 1, 1985·Canadian Journal of Biochemistry and Cell Biology = Revue Canadienne De Biochimie Et Biologie Cellulaire·U SaxenaS Mookerjea
Oct 1, 1984·Prostaglandins·M Di RosaF Russo-Marie
May 1, 1980·Proceedings of the National Academy of Sciences of the United States of America·F HirataJ Axelrod

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