Robinson C, Ellis R J
Eur J Biochem. 1984 Jul 16;142(2):343-6. doi: 10.1111/j.1432-1033.1984.tb08292.x.
The precursor of the small subunit of ribulose bisphosphate carboxylase in Pisum sativum (relative molecular mass 20 000) is processed to the mature size (relative molecular mass 14 000) by the purified processing enzyme in two steps. The maturation proceeds via an intermediate of Mr 18 000. Both processing reactions may be carried out by the same enzyme although different residues are involved in the two cleavage sites. The second cleavage is inhibited if the precursor is pre-incubated with iodoacetate. The processing intermediate cannot be detected during the uptake of the precursor by intact isolated chloroplasts but iodoacetate-treated precursor is taken up and converted to a number of polypeptides of Mr 18 000 and below.
豌豆中核酮糖二磷酸羧化酶小亚基的前体（相对分子质量为20000）经纯化的加工酶分两步加工成成熟大小（相对分子质量为14000）。成熟过程通过一个相对分子质量为18000的中间体进行。尽管两个切割位点涉及不同的残基，但两个加工反应可能由同一种酶催化。如果前体与碘乙酸预先温育，第二次切割会受到抑制。在完整分离的叶绿体摄取前体的过程中无法检测到加工中间体，但经碘乙酸处理的前体被摄取并转化为一些相对分子质量为18000及以下的多肽。
