Nakano K, Tashiro Y, Kikumoto Y, Tagaya M, Fukui T
J Biol Chem. 1986 Jun 25;261(18):8224-9.
Amino acid sequence analysis of the cyanogen bromide peptides of potato alpha-glucan phosphorylase was undertaken for comparison with rabbit muscle glycogen phosphorylase and for elucidation of the structural bases for the differences in the catalytic and regulatory properties between the animal and plant enzymes. The potato enzyme was carboxymethylated and cleaved with cyanogen bromide. The 17 distinct fragments produced were isolated by a combination of gel filtration, sulfopropyl ion exchange chromatography, and high performance liquid chromatography. The molecular weights of these fragments are distributed in a range of 300 to 30,000. Fragment CI has a blocked amino terminus, and has the same amino acid sequence as CII, which has been assigned as the amino-terminal fragment of potato phosphorylase. The blocking group was deduced to be an acetyl group from the results of fast atom bombardment mass spectrometry of an amino-terminal pentapeptide. This paper describes the sequence determination of all the cyanogen bromide fragments of potato phosphorylase. The complete structure is presented in the following paper (Nakano, K., and Fukui, T. (1986) J. Biol. Chem. 261, 8230-8236).
对马铃薯α-葡聚糖磷酸化酶的溴化氰肽进行氨基酸序列分析，以便与兔肌糖原磷酸化酶进行比较，并阐明动植物酶在催化和调节特性上存在差异的结构基础。将马铃薯酶进行羧甲基化处理，并用溴化氰裂解。通过凝胶过滤、磺丙基离子交换色谱和高效液相色谱相结合的方法，分离出产生的17个不同片段。这些片段的分子量分布在300至30,000的范围内。片段CI的氨基末端被封闭，其氨基酸序列与CII相同，CII已被指定为马铃薯磷酸化酶的氨基末端片段。通过对氨基末端五肽的快原子轰击质谱分析结果推断，封闭基团为乙酰基。本文描述了马铃薯磷酸化酶所有溴化氰片段的序列测定。完整结构见后续论文（中野，K.，和福井，T.（1986年）《生物化学杂志》261，8230 - 8236）。
