Lin J Y, Hsieh Y S, Chu S C
Institute of Biochemistry, College of Medicine, National Taiwan University, Taipei, R.O.C.
Biochem Int. 1989 Aug;19(2):313-23.
Abrin B chain and trypsin inhibitor isolated from Acacia confusa (ACTI) were covalently linked to form a chimeric protein (ANB-ACTI) with N-succinimidyl-3-(-2-pyridyldithio)propionate. The chimeric protein had 31% of trypsin inhibitory activity of ACTI and 7% of hemagglutinating activity of abrin B chain, but no inhibition on protein biosynthesis. ANB-ACTI had strong inhibitory effects on the growth of sarcoma 180 cells and Hela cell culture while the mixture of an equivalent amount of free abrin B chain and ACTI did not. The results suggests that abrin B chain of chimeric protein may act as a vector to carry ACTI into the tumor cells. ACTI into the tumor cells. ACTI in the chimeric protein potentiates its antitumor activity as well as its resistance to tryptic digestion.
相思子毒素B链与从台湾相思树中分离出的胰蛋白酶抑制剂(ACTI)通过N-琥珀酰亚胺基-3-(-2-吡啶二硫基)丙酸共价连接,形成嵌合蛋白(ANB-ACTI)。该嵌合蛋白具有ACTI 31%的胰蛋白酶抑制活性和相思子毒素B链7%的血凝活性,但对蛋白质生物合成无抑制作用。ANB-ACTI对肉瘤180细胞和Hela细胞培养物的生长具有强烈抑制作用,而等量游离相思子毒素B链和ACTI的混合物则无此作用。结果表明,嵌合蛋白中的相思子毒素B链可能作为载体将ACTI携带至肿瘤细胞中。嵌合蛋白中的ACTI增强了其抗肿瘤活性以及对胰蛋白酶消化的抗性。