Kolb E, Hudson P J, Harris J I
Eur J Biochem. 1980 Jul;108(2):587-97. doi: 10.1111/j.1432-1033.1980.tb04754.x.
The entire amino acid sequence of the protein subunit of phosphofructokinase from Bacillus stearothermophilus has been established mainly by sequence analysis of cyanogen bromide fragments and of peptides derived from these fragments by further digestion with proteolytic enzymes. Overlaps of the cyanogen bromide fragments as well as peptide sequences necessary to complement and to confirm tentative assignments within the larger peptide fragments were obtained from the sequences of selected peptides isolated from tryptic and chymotryptic digests of the intact S-[14C]-carboxymethylated protein. Sequence information was also provided by automated sequence analysis of the intact protein subunit and of some of the larger peptide fragments. The sequence is as follows: (See Text).
嗜热脂肪芽孢杆菌磷酸果糖激酶蛋白质亚基的完整氨基酸序列主要通过对溴化氰片段以及这些片段经蛋白水解酶进一步消化得到的肽段进行序列分析来确定。从完整的S-[14C]-羧甲基化蛋白质的胰蛋白酶和糜蛋白酶消化产物中分离出的选定肽段序列,获得了溴化氰片段的重叠部分以及补充和确认较大肽段内初步归属所需的肽段序列。完整蛋白质亚基和一些较大肽段的自动序列分析也提供了序列信息。序列如下:(见正文)