Article
Mutant rat phosphatidylinositol/phosphatidylcholine transfer proteins specifically defective in phosphatidylinositol transfer: implications for the regulation of phospholipid transfer activity.
Proceedings of the National Academy of Sciences of the United States of America - 12 Sept 1995
Alb J G, Gedvilaite A, Cartee R T, Skinner H B, Bankaitis V A
Abstract excerpt
The mammalian phosphatidylinositol/phosphatidylcholine transfer proteins (PI-TPs) catalyze exchange of phosphatidylinositol (PI) or phosphatidylcholine (PC) between membrane bilayers in vitro. We find that Ser-25, Thr-59, Pro-78, and Glu-248 make up a set of rat (r) PI-TP residues, substitution of which effected a dramatic reduction in the relative specific activity for PI transfer activity without significant...
Topics
- Androgen-Binding Protein
- Animals
- Base Sequence
- Carrier Proteins
- Membrane Proteins
- Models, Biological
- Molecular Sequence Data
- Mutation
- Phosphatidylcholines
- Phosphatidylinositols