Chen R, Krämer C, Schmidmayr W, Chen-Schmeisser U, Henning U
Biochem J. 1982 Apr 1;203(1):33-43. doi: 10.1042/bj2030033.
In the outer membrane of Gram-negative bacteria hydrophilic pores exist, allowing the diffusion of various low-molecular-weight solutes. These pores are formed by proteins, the porins. In a preliminary communication [Chen, Krämer, Schmidmayr & Henning (1979) Proc. Natl. Acad. Sci. U.S.A. 76, 5014-5017] we presented the primary structure of one of these porins, the 340-amino-acid-residue protein I (ompF protein) from Escherichia coli B/r. In the present paper we give the experimental evidence for this sequence. Two tryptophan positions, one valine position, two aspartic acid positions and nine out of 82 amide determinations have been corrected. To aid further studies on this class of transmembrane proteins, the isolation of most of the constituent peptides is documented.
在革兰氏阴性菌的外膜中存在亲水性孔道，允许各种低分子量溶质扩散。这些孔道由蛋白质（孔蛋白）形成。在一篇初步通讯中[陈、克雷默、施密德迈尔和亨宁（1979年）《美国国家科学院院刊》76，5014 - 5017]，我们展示了其中一种孔蛋白的一级结构，即来自大肠杆菌B/r的由340个氨基酸残基组成的蛋白质I（ompF蛋白）。在本文中，我们给出了该序列的实验证据。两个色氨酸位置、一个缬氨酸位置、两个天冬氨酸位置以及82个酰胺测定中的9个已得到校正。为有助于对这类跨膜蛋白进行进一步研究，记录了大多数组成肽段的分离情况。
