胶质原纤维酸性蛋白可溶性免疫活性肽的分离与鉴定

Biochimica et Biophysica Acta (BBA) - Protein Structure Pub Date : 1981-09-29 DOI:10.1016/0005-2795(81)90001-5

Bor-shyue Hong , Peter F. Davison

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引用次数: 18

摘要

采用Sephacryl S-200凝胶过滤，DEAE-Bio-gel A层析，从不溶性5万道顿胶质原纤维酸性蛋白的溴化氰消化液中分离得到分子量为16 000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等方法确定了多肽的均匀性。该多肽与兔抗体对完整胶质原纤维酸性蛋白产生免疫交叉反应。该肽的pI值为5.32。测定了小牛肽氨基端28个残基的氨基酸序列。

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Isolation and characterization of a soluble, immunoactive peptide of glial fibrillary acidic protein

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 electrophoresis and isoelectric focusing. The peptide from several species showed immunocrossreaction with rabbit antibody to intact glial fibrillary acidic protein. The peptide has a $p I$ value of 5.32. The amino acid sequence of 28 residues from the amino terminus of the calf peptide has been determined.

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Biochimica et Biophysica Acta (BBA) - Protein Structure

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