Nexø E, Jørgensen P E, Thim L, Roepstorff P
Department of Clinical Chemistry, Central Hospital, Hillerød, Denmark.
Biochim Biophys Acta. 1990 Mar 1;1037(3):388-93. doi: 10.1016/0167-4838(90)90041-d.
Two forms of epidermal growth factor (EGF) have been purified to homogeneity from rat urine by immunoaffinity chromatography and gel filtration. For one of the purified peptides the molecular mass has been determined to be 5891 by mass spectrometry. This peptide consists of 51 amino acid residues. The sequence of the first 48 amino acid residues is identical to the previously published sequence for submandibular rat EGF. The C-terminal three residues (49-51) are Trp-Trp-Lys. The other purified peptide has a molecular mass of 45 kDa as determined by SDS-polyacrylamide gel electrophoresis. The N-terminal sequence is Asn-Tyr-Lys-Asp-(Cys)-Gly-Pro-Gly-Gly-(Cys)-Gly-Ser-His-Ala. Both the high and the low molecular mass form of urinary rat EGF are able to bind to the human placenta receptor for EGF.
通过免疫亲和层析和凝胶过滤从大鼠尿液中已将两种形式的表皮生长因子（EGF）纯化至同质。对于其中一种纯化的肽，通过质谱测定其分子量为5891。该肽由51个氨基酸残基组成。前48个氨基酸残基的序列与先前发表的大鼠颌下腺EGF序列相同。C末端的三个残基（49 - 51）为色氨酸-色氨酸-赖氨酸。另一种纯化的肽通过SDS-聚丙烯酰胺凝胶电泳测定分子量为45 kDa。其N末端序列为天冬酰胺-酪氨酸-赖氨酸-天冬氨酸-（半胱氨酸）-甘氨酸-脯氨酸-甘氨酸-甘氨酸-（半胱氨酸）-甘氨酸-丝氨酸-组氨酸-丙氨酸。大鼠尿液中EGF的高分子量和低分子量形式均能与人胎盘EGF受体结合。
