Primary structure of yeast cytochrome c peroxidase. I. Chemical characterization of the polypeptide chain and of tryptic and chymotryptic peptides.
Primary structure of yeast cytochrome c peroxidase. I. Chemical characterization of the polypeptide chain and of tryptic and chymotryptic peptides.
复制标题
酵母细胞色素c过氧化物酶的一级结构。
DOI：
10.1016/0003-9861(80)90218-0
复制
发表时间：
1980
影响因子：
3.9
通讯作者：
Yonetani,T
中科院分区：
文献类型：
--
作者：
Takio,K;Yonetani,T
The amino acid composition of yeast cytochromecperoxidase was determined and calculated assuming that the enzyme contained one protoheme per molecule. On the basis of the amino acid composition and heme content the minimumMrwas calculated to be 35,235. Gel electrophoresis in the presence of sodium dodecyl sulfate indicated the presence of a single polypeptide chain with aMrof approximately 33,000. A single cysteinyl residue present in the molecule was shown to be resistant against reaction with iodoacetic acid in the native form of both holo- and apo-enzymes, but readily modified with the reagent in the denatured form. Automated Edman degradation yielded an aminoterminal sequence of 11 residues beginning with threonine. Twenty-eight tryptic and 47 chymotryptic peptides were isolated from the carboxymethylated apoprotein and subjected to the sequence analysis by the dansyl-Edman method. The results with these peptides confirmed and extended the amino- and carboxyl-terminal sequences and in addition provided a partial sequence covering approximately 90% of the polypeptide chain.
