Lipkin V M, Obukhov A N, Bogachuk A P, Telezhinskaia I N, Shemiakin V V
Bioorg Khim. 1985 Nov;11(11):1481-92.
The alpha- and beta-subunits of the GTP-binding protein (transducin) from cattle retina were cleaved with cyanogen bromide. 21 peptides covering 90-100% of the amino acid sequence of the alpha- and beta-subunits were isolated from the hydrolyzate. Cyanogen bromide peptides complete or partial amino acid sequence was determined, the results were compared with those by Numa and coworkers [1] and Lochrie et al. [2] at the primary structure of the transducin alpha-subunit deduced from the nucleotide sequence of the cDNA. The structure by Lochrie is shown to differ much from the true structure of the alpha-subunit; probably, the investigators isolated cDNA, corresponding to the gene for some GTP-binding protein homologous to transducin, but not to the gene for the transducin alpha-subunit. The Numa's structure also contains an error. The final primary structure of the transducin alpha-subunit is given. The protein polypeptide chain consists of 349 amino acid residues and has an acetylmethionine residue as the N-terminal residue.
用溴化氰裂解牛视网膜中GTP结合蛋白（转导素）的α和β亚基。从水解产物中分离出覆盖α和β亚基氨基酸序列90 - 100%的21个肽段。测定了溴化氰肽段的全部或部分氨基酸序列，并将结果与沼田等人[1]以及洛奇里等人[2]根据cDNA核苷酸序列推导的转导素α亚基一级结构的结果进行了比较。结果表明，洛奇里提出的结构与α亚基的真实结构有很大差异；可能这些研究者分离出的cDNA对应的是与转导素同源的某种GTP结合蛋白的基因，而非转导素α亚基的基因。沼田提出的结构也存在一个错误。给出了转导素α亚基的最终一级结构。该蛋白质多肽链由349个氨基酸残基组成，N端残基为乙酰甲硫氨酸残基。
