Phosphatidylcholine Exchange Protein from Beef Liver

Kamp, H.H.; Wirtz, K.W.A.

doi:10.1038/newbio246102a0

Cited by 122 publications

(39 citation statements)

References 19 publications

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“…Several reports have stated that the PI-transfer protein has a large preference for transferring PI over PC (i.e., approximately 10-fold faster) [4,5,28], while transfer of other lipid species was either very low (i.e., phosphatidylglycerol and sphingomyelin), or completely absent (i.e., phosphatidylethanolamine, phosphatidylserine, phosphatidic acid and cardiolipin) (Somerharju et al [6]). Chemical modification of PI indicated that the PI-transfer protein absolutely requires the intact inositol ring for the lipid to be preferentially transferred.…”

Section: Discussionmentioning

confidence: 99%

Binding of phospholipids to the phosphatidylinositol transfer protein from bovine brain as studied by steady-state and time-resolved fluorescence spectroscopy

Paridon

Visser

Wirtz

1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The phosphatidylinositoi transfer protein isolated from brain, liver, heart and platelets was found to be present in two subforms which could be distinguished on the basis of the isoelectric points. In this study we have demonstrated that the two subforms isolated from bovine brain are due to the presence of either phosphatidylinositol or phosphatidylcholine in the lipid binding site of the protein. The transfer protein accommodates one phosphatidylinositol molecule in the binding site. The binding site for the sn-2 fatty acyi chain was investigated by incorporating in the transfer protein either phosphatidylinositol or pbosphatidylcholine carrying a parinaroyi-chain attached at the sn-2 position. Time-resolved fluorescence spectroscopy revealed that the sn-2 fatty acyl chains for both phospholipids in the lipid-protein complex were completely immobilized (i.e., rotational correlation times of 17.4 ns for phosphatidylcholine and 16.3 ns for phosphatidylinositol). The similarity in correlation times suggests that the sn-2 fatty acyl chains of both phospholipids are accommodated in the same hydrophobic binding site of the protein.

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Section: Discussionmentioning

confidence: 99%

Binding of phospholipids to the phosphatidylinositol transfer protein from bovine brain as studied by steady-state and time-resolved fluorescence spectroscopy

Paridon

Visser

Wirtz

1987

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…Extraction of bovine liver PC-TP by organic solvents showed that one PC-TP molecule contains one molecule of non-covalently bound PC [2,7]. These data indicate that PC-TP has a binding cavity for PC.…”

Section: Introductionmentioning

confidence: 84%

Phosphatidylcholine transfer protein from bovine liver contains highly unsaturated phosphatidylcholine species

et al. 1996

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“…A 1.5 X 1.5-cm extended corner with a hole of 0.8 cm was used to add protein and/or vesicles to the subphase. In the absence of a monolayer the protein collected at the air-water interface until a final pressure of 12.5 mN m-l was reached (Demel et al, 1973). The protein penetrated a 16:0/18:1 PC monolayer provided the initial lipid film pressure was below 20 mN m-l.…”

Section: Phosphatidylcholine Transfer Protein (Pc-tp)mentioning

confidence: 99%