Purification and characterisation of a non-specific lipid transfer protein from goat liver.
A non-specific lipid transfer protein has been purified from the pH 5.1 supernatant of goat liver by DEAE-cellulose, CM-cellulose and Sephadex G-75 column chromatography. The protein shows a single band on polyacrylamide gel electrophoresis and transfers 450 nmol of phosphatidylcholine per min per mg of protein under the present assay condition. This protein has a subunit molecular weight of 12,000 and an isoelectric point of 8.65. Amino acid analysis reveals the absence of methionine. Histidine has been identified as the only N-terminal amino acid. Besides phosphatidylcholine, the protein transfers phosphatidylinositol, phosphatidylethanolamine, phosphatidylserine and cholesterol. Chemical modification studies showed the involvement of free amino and thiol groups in the maintenance of the transfer activity of the goat liver protein.
Basu
J
J
Department of Chemistry, Bose Institute, Calcutta, India.
Kundu
M
M
Bhattacharya
U
U
Mazumder
C
C
Chakrabarti
P
P
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D002784:Cholesterol / Q000378:metabolism*; D006041:Goats; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D007700:Kinetics; D050356:Lipid Metabolism; D008081:Liposomes; D008099:Liver / Q000032:analysis*; D008861:Microsomes / Q000378:metabolism; D008970:Molecular Weight; D013379:Substrate Specificity
D000596:Amino Acids; D002352:Carrier Proteins; D008081:Liposomes; C030363:lipid transfer protein; D002784:Cholesterol