Celada F, Fowler A V, Zabin I
Biochemistry. 1978 Nov 28;17(24):5156-60. doi: 10.1021/bi00617a014.
Antibodies were prepared against 18 tryptic and cyanogen bromide peptides from beta-galactosidase ranging in size from 15 to 96 amino acid residues representing more than 80% of the polypeptide chain. They were tested for binding capacity and affinity toward their homologous antigens and toward the whole native protein. Nine antisera bound to beta-galactosidase; these had been raised against certain peptides from the central and carboxyl-terminal regions of the poly-peptide chain. Based on these results a preliminary model of the three-dimensional structure of the folded protein is suggested.
针对来自β-半乳糖苷酶的18种胰蛋白酶和溴化氰肽制备了抗体,这些肽的大小在15至96个氨基酸残基之间,占多肽链的80%以上。测试了它们对同源抗原和整个天然蛋白质的结合能力及亲和力。九种抗血清与β-半乳糖苷酶结合;这些抗血清是针对多肽链中央和羧基末端区域的某些肽产生的。基于这些结果,提出了折叠蛋白三维结构的初步模型。