THE PRIMARY STRUCTURE OF A BASIC (PI-9.0) FATTY-ACID-BINDING PROTEIN FROM LIVER OF GALLUS-DOMESTICUS
THE PRIMARY STRUCTURE OF A BASIC (PI-9.0) FATTY-ACID-BINDING PROTEIN FROM LIVER OF GALLUS-DOMESTICUS
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DOI：
10.1016/0305-0491(94)90010-8
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发表时间：
1994-10-01
影响因子：
2.2
通讯作者：
SPADON, P
中科院分区：
文献类型：
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作者：
CECILIANI, F;MONACO, HL;SPADON, P
从家鸡肝脏中分离纯化出一种碱性(等电点为9.0)的脂肪酸结合蛋白，用自动Edman降解方法测定了该蛋白的氨基酸全序列。该蛋白质含有125个氨基酸残基，相对分子质量为14094。要鉴定模拟的N-末端Ac-Ala，需要在序列分析之前用酰基氨基酸释放酶消化SV-8肽。序列比较表明，鸡肝碱性FABP与其他属于细胞内脂分子结合蛋白超家族的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与其底物的结合方式可能略有不同。BASIC-FABP已提交给EMBL数据库，登录号为P80226。
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 Mocked 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.