[Effect of water soluble non-membrane proteins on the phospholipid structure].
The interaction of water-soluble nonmembraneous proteins (trypsin and the basic pancreatic trypsin inhibitor (BPTI)) with soybean phospholipids was studied using multilamellar vesicles. Multilamellar vesicles were obtained from soybean lipid extracts and mixtures of individual phospholipids based on phosphatidylcholine. These mixtures contain different phospholipids: "bilayer", "nonbilayer", and negatively charged. It was shown that the content of both proteins in the complex depends on pH and the presence of negatively charged components. On the basis of this finding, the conclusion about the electrostatic nature of lipid-protein interaction was made. The structural organization of soybean phospholipids in multilamellar vesicles was studied in the presence and absence of the proteins using broad-line 31P-NMR spectroscopy. It was found that, in mixtures of phospholipids of complex composition, different types of phases coexist, and phospholipids of different classes can compensate the effects of each other. Trypsin and BPTI affect the structure of phospholipids in a similar way, inducing considerable structural changes in multilamellar vesicles of preparations containing negatively charged components in whose structure there coexisted primordially the bilayer and isotropic phases.
Sorokoumova
G M
GM
Lomonosov Academy of Fine Chemical Technology, pr. Vernadskogo 84, Moscow, 117571 Russia.
Selishcheva
A A
AA
Tiurina
O P
OP
Alekseeva
S G
SG
Martynova
O M
OM
Sharf
T V
TV
Shvets
V I
VI
D000818:Animals; D007611:Aprotinin / Q000737:chemistry*; D002417:Cattle; D002855:Chromatography, Thin Layer; D009682:Magnetic Resonance Spectroscopy; D008297:Male; D010743:Phospholipids / Q000737:chemistry*; D012995:Solubility; D013025:Glycine max; D014357:Trypsin / Q000737:chemistry*; D014867:Water
D010743:Phospholipids; D014867:Water; D007611:Aprotinin; D014357:Trypsin