부산대학교 도서관

In this study a novel heat-stable lipid transfer protein, designated Mc LTP 1 , was purified from noni ( Morinda citrifolia L.) seeds, using four purification steps which resulted in a high-purified protein yield (72 mg Mc LTP 1 from 100 g of noni seeds). Mc LTP 1 exhibited molecular masses of 9.450 and 9.466 kDa, determined by electrospray ionisation mass spectrometry. The N-terminal sequence of Mc LTP 1 (AVPCGQVSSALSPCMSYLTGGGDDPEARCCAGV), as analysed by NCBI-BLAST database, revealed a high degree of identity with other reported plant lipid transfer proteins. In addition, this protein proved to be resistant to pepsin, trypsin and chymotrypsin digestion. Mc LTP 1 given intraperitoneally (1, 2, 4 and 8 mg/kg) and orally (8 mg/kg) caused an inhibition of the writhing response induced by acetic acid in mice. This protein displayed thermostability, retaining 100% of its antinociceptive activity after 30 min incubation at 80 °C. Pretreatment of mice with Mc LTP 1 (8 mg/kg, i.p. and p.o.) also decreased neurogenic and inflammatory phases of nociception in the formalin test. Naloxone (2 mg/kg, i.p.) antagonised the antinociceptive effect of Mc LTP 1 suggesting that the opioid mechanisms mediate the analgesic properties of this protein. [ABSTRACT FROM AUTHOR]