Godovac-Zimmermann J, Conti A, James L, Napolitano L
Department of Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra.
Biol Chem Hoppe Seyler. 1988 Mar;369(3):171-9. doi: 10.1515/bchm3.1988.369.1.171.
The complete primary structure of donkey beta-lactoglobulin I was determined by pulsed-liquid phase microsequencing of tryptic peptides. The protein has been isolated in monomeric form and it corresponds to monomeric beta-lactoglobulin of type I. With the inclusion of donkey beta-lactoglobulin I there are 13% common residues amongst the members of the beta-lactoglobulin family. Donkey beta-lactoglobulin I is homologous to the retinol-binding protein, bilin-binding protein and five other proteins belonging to the new superfamily of hydrophobic molecule transporters. A rapid method for peptide isolation and the strategy for microsequencing of this protein have been described.
通过对胰蛋白酶肽段进行脉冲液相微量测序，确定了驴β-乳球蛋白I的完整一级结构。该蛋白质已以单体形式分离出来，它对应于I型单体β-乳球蛋白。包括驴β-乳球蛋白I在内，β-乳球蛋白家族成员中有13%的共同残基。驴β-乳球蛋白I与视黄醇结合蛋白、胆绿素结合蛋白以及属于疏水分子转运蛋白新超家族的其他五种蛋白质同源。已描述了一种肽段分离的快速方法以及该蛋白质的微量测序策略。
