Hong B S, Davison P F
Biochim Biophys Acta. 1981 Sep 29;670(2):139-45. doi: 10.1016/0005-2795(81)90001-5.
A soluble immunoactive peptide with a molecular weight of 16 000 was isolated and purified from the cyanogen bromide digest of the insoluble 50 000 dalton glial fibrillary acidic protein by Sephacryl S-200 gel filtration followed by DEAE-Bio-gel A chromatography. The homogeneity of the peptide was established by SDS-polyacrylamide gel electrohporesis and isoelectric focusing. The peptide from several species showed immunocrossreaction with rabbit antibody to intact glial fibrillary acidic protein. The peptide has a pI value of 5.32. The amino acid sequence of 28 residues from the amino terminus of the calf peptide has been determined.
通过Sephacryl S - 200凝胶过滤，随后进行DEAE - Bio - gel A柱层析，从分子量为50000道尔顿的不溶性胶质纤维酸性蛋白的溴化氰消化物中分离并纯化出一种分子量为16000的可溶性免疫活性肽。通过SDS - 聚丙烯酰胺凝胶电泳和等电聚焦确定了该肽的均一性。来自几个物种的该肽与兔抗完整胶质纤维酸性蛋白抗体显示出免疫交叉反应。该肽的pI值为5.32。已经确定了小牛肽氨基末端28个残基的氨基酸序列。
