secretory protein meaning in Chinese
分泌蛋白
Examples
- So the study of the microstructure of ers , especially the studies of membrane proteins , secretory proteins and molecular chaperones synthesized by ers have become the frontiers of the molecular biology all over the world
因此研究内质网的微细结构，尤其是er合成的膜蛋白、分泌蛋白和分子伴侣已成为国际上的前沿课题。 - Hydrophobicity analysis predicted a 36 - residue hydrophobic signal peptide for secretion in the n - terminus , and no transmembrane region was present , suggesting it might be a type of secretory protein . some generic and atipical n - glycosylation sites were present in clsp , suggesting that the protein might represent a glycoprotein . the clsp protein contained one cub ( clr / cls , an embryonic sea urchin protein uegf , and bone morphogenetic protein i ) domain from 39th to 164th ammo acids , which is known to be involved in protein - protein or protein - substrate interaction , and a trypsin - like serine protease domain positioned from 244th to 483rd amino acids
Clsp分子具有补体样丝氨酸蛋白酶的多种结构特征，包括36个氨基酸组成的疏水信号肤，一个cub ( clr / cls ， anembryonicseaurehinproteinuegf ， andbonemorphogeneticproteinl )结构域和一个胰酶样丝氨酸蛋白酶结构域( t汀psin一likeserineproteasedomain )和几个保守的糖基化位点等，没有发现有跨膜区的存在。 - The hwtx - i gene was chemically synthesized according to its known cdna sequence , the gene was inserted into vector ppic9k which contained aoxj promotor and the sequence of a secreting signal peptide - a - factor , the cloning ppic9k / hwtx - i was constructed and confirmed by two - step pcr and dna sequence analysis , then it was transformed into host strain gs115 , a his + muts cell line was screened and multicopy transformants were screened by various g418 concentrations , the multicopy transformant was named gh1 . gh1 was cultivated in flasks . after 6 days of induction by 0 . 5 % methanol , the supernatant was checked by 16 . 5 % tricine - sds page , which showed there was a band in the position of 3 . 5 - 6 . 1kd , then it was isolated and desalted by ultrofiltration followed by ion exchange of cm column , after reverse phase hplc of ci8 and vacuum drying , the purified rhwtx - 1 was obtained which was proved to be correct recombinant hwtx - i by tricine sds - page , maldi - tof mass spectrometry , amino acid composition analysis , the n - terminal amino acid sequence and its biological activity , the final field of the purified rhwtx - i was about 80mg / l , accounting for 23 . 6 % of it total secretory proteins
将带有hwtx -基因的ppic9k经blgii线性化后，转化酵母宿主菌gs115原生质体后经筛选阳性克隆并经表型鉴定为his ~ + mut ~ s酵母菌，进一步用遗传毒素g418筛选多拷贝的转化菌株，命名为gh1 ；将gh1甲醇酵母菌用0 . 5的甲醇诱导表达，发酵上清经90饱和度的( nh _ 4 ) _ 2so _ 4沉淀， yw - 3 ( mwc03000 )的超滤膜超滤，再经cm阳离子交换， c _ ( 18 )反相hplc纯化得到分子量为4kd左右的组分，其中4289 . 05的组分经质谱鉴定，氨基酸组成分析和序列测定为正确的表达产物，生物学活性表明其活性为天然毒素活性70 % ，表达量为80mg / l 。