Ceciliani F, Monaco H L, Ronchi S, Faotto L, Spadon P
Istituto di Fisiologia Veterinaria e Biochimica, Università di Milano, Italy.
Comp Biochem Physiol B Biochem Mol Biol. 1994 Oct-Nov;109(2-3):261-71. doi: 10.1016/0305-0491(94)90010-8.
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.
通过对胰蛋白酶、溴化氰/氢氟酸苯甲酰化（CNBr/HFBA）和金黄色葡萄球菌蛋白酶肽段进行自动Edman降解，测定了从家鸡肝脏中纯化得到的一种碱性（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，对应分子量为14094。在进行序列分析之前，需要用酰基氨基酸释放酶消化SV-8肽段，以鉴定封闭的N端乙酰丙氨酸（Ac-Ala）。序列比较表明，鸡肝脏碱性脂肪酸结合蛋白（basic-FABP）与属于细胞内脂质分子结合蛋白超家族的其他蛋白质具有显著相似性。此外，这些序列数据证实，与其他脂肪酸结合蛋白相比，碱性脂肪酸结合蛋白可能以略有不同的方式结合其底物。碱性脂肪酸结合蛋白已提交至EMBL数据库，登录号为P80226。
