Abstract

A system for the isolation of human plasma lipid transfer protein (LTP) has been devised using a combination of conventional and high-performance ion-exchange chromatography. Following initial purification by ammonium sulphate precipitation, ultracentrifugation, hydrophobic interaction and cation-exchange chromatography, appropriate fractions were further purified using the Pharmacia fast protein liquid chromatography system. Using this method of purification, human plasma LTP has been purified more rapidly and with greater recovery than with conventional column chromatography. Whereas two forms of LTP were previously reported from the authors' laboratory [LTP-I, molecular mass ( M r) 69 000 and LTP-II, M r 55 000], with an improved chromatographic system only one form of LTP (LTP-I) has been isolated. This suggests that LTP-II may have been a fragment of LTP-I, produced during the previously used lengthy purification process.

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