Hara K, Hsu Chen C J, Sonenberg M
Biochemistry. 1978 Feb 7;17(3):550-6. doi: 10.1021/bi00596a028.
Two bovine growth hormone peptides containing residues 96 to 133 in one and a larger peptide corresponding to residues 1 to 95 and 151 to 191 linked by a disulfide bond have been recombined. Recombination was performed in 1.0 N acetic acid without and with 8 M urea and the recombined peptides were purified by gel filtration. Evidence of recombination of the peptides has been established by gel filtration, polyacrylamide gel disc electrophoresis, amino acid composition, ultraviolet absorption, circular dichroism, and intrinsic fluorescence. The molar growth promoting activity of the recombined peptides measured by tibial width assay in hypophysectomized rats was 10% that of the native hormone and greater than the sum (1%) of the growth promoting activities of the individual peptides. These studies suggest that some contribution of the larger peptide is necessary for more complete expression of the growth promoting activity of the bovine growth peptide corresponding to residues 96 to 133.
已将两种牛生长激素肽进行了重组。其中一种含有96至133位的残基，另一种较大的肽对应于1至95位以及151至191位的残基，二者通过二硫键相连。重组在1.0 N乙酸中进行，分别在无8 M尿素和有8 M尿素的条件下进行，重组后的肽通过凝胶过滤进行纯化。已通过凝胶过滤、聚丙烯酰胺凝胶圆盘电泳、氨基酸组成、紫外吸收、圆二色性和内源荧光确定了肽的重组证据。通过胫骨宽度测定法在垂体切除的大鼠中测量，重组肽的摩尔促生长活性为天然激素的10%，且大于单个肽促生长活性之和（1%）。这些研究表明，较大的肽对于更完整地表达对应于96至133位残基的牛生长肽的促生长活性有一定贡献。
