Fattoum A, Roustan C, Feinberg J, Desvages G, Pradel L A
Eur J Biochem. 1978 Jan 2;82(1):161-7. doi: 10.1111/j.1432-1033.1978.tb12007.x.
Cyanogen bromide cleavage of yeast 3-phosphoglycerate kinase yielded four fragments which account for the amino acid composition of the entire molecule. These results are consistent with a single polypeptide chain of molecular weight 42 000. Affinity chromatography on Sepharose-mercurial followed by gel filtration on Sephadex was used with success for separation of peptides. The carboxyl and N-terminal fragments were characterized. The N-terminal fragment contained the single cysteinyl residue of the protein. After cyanylation and subsequent cleavage, this cysteinyl residue was located near position 100.
用溴化氰裂解酵母3-磷酸甘油酸激酶产生了四个片段，这些片段说明了整个分子的氨基酸组成。这些结果与分子量为42000的单条多肽链相符。先后使用琼脂糖-汞亲和层析和葡聚糖凝胶过滤成功地分离了肽段。对羧基末端和N末端片段进行了表征。N末端片段含有该蛋白质唯一的半胱氨酰残基。在氨甲酰化并随后裂解后，该半胱氨酰残基位于第100位附近。
