Karplus P A, Walsh K A, Herriott J R
Biochemistry. 1984 Dec 18;23(26):6576-83. doi: 10.1021/bi00321a046.
The amino acid sequence of spinach ferredoxin: NADP+ oxidoreductase was determined by using overlapping sets of peptides derived by cleavage at arginyl or methionyl residues. The protein from different preparations varied in its length at the amino terminus. In the longest form the amino terminus is blocked with a pyroglutamyl residue, as determined by NMR. A single disulfide bond was placed between cysteine residues 132 and 137. The 314-residue sequence corresponds to a molecular weight of 35 317. The carboxyl-terminal half of the sequence has been fit to the electron density map of the NADP binding domain, revealing that this portion of the chain forms a typical nucleotide binding fold.
通过使用在精氨酰或甲硫氨酰残基处裂解产生的重叠肽段组，确定了菠菜铁氧化还原蛋白：NADP⁺氧化还原酶的氨基酸序列。来自不同制备物的蛋白质在氨基末端的长度有所不同。通过核磁共振确定，在最长形式中，氨基末端被焦谷氨酰残基封闭。在半胱氨酸残基132和137之间存在一个二硫键。314个残基的序列对应的分子量为35317。该序列的羧基末端一半已与NADP结合结构域的电子密度图拟合，表明该链的这一部分形成了典型的核苷酸结合折叠。
