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The analysis of chemical stoucure and homology peptides on hunan e*rly pregrax pactor

湖南益利灵肽化学成分及同源肽分析

基本信息

批准号：
04671020
负责人：
SUEOKA Kou
金额：
$ 1.28万
依托单位：
Keio University
依托单位国家：
日本
项目类别：
Grant-in-Aid for General Scientific Research (C)
财政年份：
1992
资助国家：
日本
起止时间：
1992 至 1993
项目状态：
已结题

来源：
https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-04671020/
关键词：
EPF Rosette inhibition test SDS-PAGE glycoprotein FPLC Thieredoxin SDS‐PAGE SDSーPAGE

项目摘要

The complete purification and determination of the chemical structure of early pergnancy factor (EPF) has been performed to elucidate the essential role of EPF in the mechanisms of establishment of pregnancy. The purified property from the source of human urine from pregnant women has been determined amino acid sequences from N-terminal of its peptide. This purified EPF had a strong homology with the precusor of human epidermal growth factor. The other purified property of EPF from the extract of human placenta had been recently reported by Clarke et al., whtich had the identified sequences with Thioredoxin (Adult type T cell leukemia factor ; ADF). In order to identifu these two EPF properies, the polyclonal antibodies has been made by immunizing synthethized peptides with parts of EPF chemical structure to the rabbit. The effects of this antibody in the responcee of biologigal activity (rosette inhibition activity), serological responces (dot blot, ELISA), and biochemical determination. From these results, these two EPF properties was deonstrated completely defferent substances althugh both had sane rosette inhibition activity.

为阐明早孕因子（EPF）在妊娠形成机制中的重要作用，对EPF进行了完全纯化和化学结构测定。从孕妇尿中分离纯化得到的多肽经N-末端氨基酸序列测定，具有一定的纯化特性。纯化的EPF与人表皮生长因子的前体有很强的同源性。Clarke等人最近报道了从人胎盘提取物中纯化EPF的另一种性质，与硫氧还蛋白（Adult type T cell leukemia factor，ADF）的同源序列一致。为了鉴定EPF的这两种性质，我们用人工合成的EPF部分化学结构的多肽免疫家兔，制备了EPF的多克隆抗体。本文报道了该抗体的生物学活性（玫瑰花结抑制活性）、血清学反应（斑点杂交、ELISA）和生化测定的效果。结果表明，这两种EPF的性质完全不同，但都具有相同的抑制玫瑰花结的活性。