家鸡肝脏碱性(pI 9.0)脂肪酸结合蛋白的一级结构

Fabrizio Ceciliani , Hugo L. Monaco , Severino Ronchi , Ludovica Faotto , Paola Spadon
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引用次数: 38

摘要

通过对胰酶、CNBr/HFBA和金黄色葡萄球菌蛋白酶肽的自动Edman降解,确定了从家鸡肝脏中纯化的碱性(pI 9.0)脂肪酸结合蛋白的完整氨基酸序列。该蛋白含有125个氨基酸残基,对应的分子质量为14094。鉴定阻断的n端Ac-Ala需要在序列分析之前用乙酰氨基酸释放酶消化SV-8肽。序列比较表明,鸡肝basic-FABP与细胞内脂质分子结合蛋白超家族的其他蛋白具有显著的相似性。此外,这些序列数据证实,与其他fabp相比,basic-FABP与底物的结合方式可能略有不同。Basic-FABP提交至EMBL数据库,检索号为P80226
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The primary structure of a basic (pI 9.0) fatty acid-binding protein from liver of Gallus domesticus

The complete amino acid sequence of a basic (pI 9.0) fatty acid-binding protein purified from liver of Gallus domesticus was determined by automated Edman degradation of tryptic, CNBr/HFBA and Staphylococcus aureus protease peptides. The protein contains 125 amino acid residues which correspond to a molecular mass of 14094. The identification of the blocked N-terminus Ac-Ala required digestion of a SV-8 peptide with the acylamino acid-releasing enzyme prior to sequence analysis. Sequence comparison shows that chicken liver basic-FABP has a significant similarity to other proteins belonging to the superfamily of intracellular lipid molecule binding proteins. Moreover, these sequence data confirm that basic-FABP probably binds its substrate in a slightly different way when compared with other FABPs. Basic-FABP was submitted to the EMBL Data Library with an accession number of P80226

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