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从人和牛血清里纯化的磷脂酰肌醇-多糖-特异性磷脂酶D(PI-G PLD)能特异性水解PI-GS抛锚蛋白里磷酸肌醇键,本文作者确定了牛PI-GPLD的一级结构并研究了其功能活性.作者以来源于牛血清PI-G PLD的8个胰蛋白酶酶解片段的氨基酸序列为基础,制备4个变性寡核苷酸探针,从牛DATA文库里筛选PI-G PLD文库,能获得所有8个胰蛋白酶酶解片段的完整氨基酸序列的cDNA克隆,此克隆基因能编码817个氨基酸的成熟蛋白,Nfr为90.2kD,有8个潜在N-连结糖基化部位,其前有23个氨基酸的单一信号肽序列。氨基酸序列分析有4个内部同源区域:357～379位氨
Phosphatidylinositol-polysaccharide-specific phospholipase D (PI-G PLD), purified from human and bovine serum, specifically hydrolyzes the phosphoinositide bond in PI-GS ankyrin, and the authors identified a Level structures and their functional activities were studied.The authors prepared four denaturing oligonucleotide probes based on the amino acid sequences of eight tryptic fragments derived from the bovine serum PI-G PLD and screened from the cow DATA library The PI-G PLD library was used to obtain a cDNA clone of the complete amino acid sequence of all 8 tryptic fragments. The cloned gene encodes a mature protein of 817 amino acids with a Nfr of 90.2 kD and 8 potential N-linked glycosyls The site, preceded by a single 23 amino acid signal peptide sequence. Amino acid sequence analysis has four internal homologous regions: 357 ~ 379 ammonia