Fothergill L A, Hodgson G I
Biochem J. 1976 Feb 1;153(2):145-9. doi: 10.1042/bj1530145.
The molecular weight and amino acid composition of phosphoglycerate mutase from yeast were determined. CNBr cleavage produced a large (190-residue) fragment and a small (60-residue) fragment. Tryptic and chymotryptic peptides derived from the large fragment were fractionated by ion-exchange chromatography. Peptides from two histidine-containing regions were isolated and the amino acid sequences were determined. Correlation of these data with X-ray-crystallographic evidence shows that the histidine residue in the sequence Arg-Leu Asn-Glu-Arg-His-Tyr-Gly-Asp-Leu-Glu-Gly-Lys is located at the active site.
测定了来自酵母的磷酸甘油酸变位酶的分子量和氨基酸组成。溴化氰裂解产生一个大的（190个残基）片段和一个小的（60个残基）片段。通过离子交换色谱法对来自大片段的胰蛋白酶和胰凝乳蛋白酶肽段进行了分离。分离出了来自两个含组氨酸区域的肽段，并测定了其氨基酸序列。这些数据与X射线晶体学证据的相关性表明，序列Arg-Leu Asn-Glu-Arg-His-Tyr-Gly-Asp-Leu-Glu-Gly-Lys中的组氨酸残基位于活性位点。
