PRIMARY STRUCTURE OF HUMAN PLACENTAL ANTICOAGULANT PROTEIN
PRIMARY STRUCTURE OF HUMAN PLACENTAL ANTICOAGULANT PROTEIN
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DOI：
10.1021/bi00399a011
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发表时间：
1987-12-15
期刊：
影响因子：
2.9
通讯作者：
FUJIKAWA, K
中科院分区：
文献类型：
--
作者：
FUNAKOSHI, T;HENDRICKSON, LE;FUJIKAWA, K
应用氨基酸和核苷酸序列测定技术，确定了人胎盘抗凝蛋白的一级结构。用溴化氰消化羧甲基化的蛋白质，并通过凝胶过滤和高效液相色谱法分离得到的肽。从7个溴化氰片段中鉴定出319个氨基酸残基中的239个。从人胎盘cDNA文库中克隆了一个编码胎盘抗凝蛋白的全长cDNA克隆。该克隆长1.6个碱基，含有编码甲硫氨酸的翻译起始位点、编码成熟蛋白的957个核苷酸、终止密码子、poly（A）识别位点和poly（A）尾。胰蛋白酶封闭的肽，从NH 2-末端的蛋白质的分析表明，末端甲硫氨酸被删除和相邻的丙氨酸残基被乙酰化的翻译后事件。胎盘抗凝蛋白由319个氨基酸组成，氨基末端为乙酰丙氨酸，与脂皮质素I和II具有高度的序列同源性。它包含四个内部重复，每个重复包括一个对应于推定的Ca 2+依赖性磷脂结合位点的序列。胎盘抗凝蛋白是脂皮质素/钙调蛋白家族的成员。
The primary structure of human placental anticoagulant protein was determined by a combination of amino acid and nucleotide sequencing techniques. The carboxymethylated protein was digested with cyanogen bromide, and the resulting peptides were separated by gel filtration and high-performance liquid chromatography. A total of 239 out of 319 amino acid residues were identified from 7 cyanogen bromide fragments. A full-length cDNA clone encoding placental anticoagulant protein was isolated from a human placenta cDNA library. This clone was 1.6 kilobases long and contained a translation initiation site coding for methionine, 957 nucleotides encoding for the mature protein, a stop codon, a poly(A) recognition site and a poly(A) tail. Analysis of the tryptic-blocked peptide that originated from the NH2-terminus of the protein showed that the terminal methionine was removed and the adjacent alanine residue was acetylated by posttranslation events. Placental anticoagulant protein is composed of 319 amino acids with acetylalanine as the NH2-terminus and has a high degree of sequence identify with lipocortins I and II. It contains four internal repeats, each including a sequence corresponding to a putative Ca2+-dependent phospholipid binding site. Placental anticoagulant protein is a member of the lipocortin/calpactin family.