Gautier M F, Alary R, Joudrier P
Laboratoire de Technologie des Céréales, INRA, Montpellier, France.
Plant Mol Biol. 1990 Mar;14(3):313-22. doi: 10.1007/BF00028768.
A Triticum durum cDNA library prepared from developing endosperm (22 days after flowering (DAF] was screened using synthetic oligonucleotide probes covering part of the CM3 and CM16 N-terminal protein sequences. A full-length cDNA clone (pTd78) encoding the CM16 protein (chloroform/methanol-soluble protein) was isolated and characterized. To our knowledge this is the first characterization of a clone coding for a wheat CM protein. The CM16 protein is synthesized as a preprotein with a signal peptide of 24 residues, the molecular weight of the mature protein being 13,438 Da. As other members of the cereal trypsin/alpha-amylase inhibitor family, the CM16 protein contains 10 cysteine residues, their position being well conserved. In developing endosperm the highest level of CM16 mRNA was detected at mid-maturation.
利用覆盖CM3和CM16 N端蛋白质序列部分区域的合成寡核苷酸探针，对从发育中的胚乳（开花后22天）制备的硬粒小麦cDNA文库进行筛选。分离并鉴定了一个编码CM16蛋白（氯仿/甲醇可溶性蛋白）的全长cDNA克隆（pTd78）。据我们所知，这是首次对编码小麦CM蛋白的克隆进行表征。CM16蛋白以前体蛋白形式合成，带有一个24个残基的信号肽，成熟蛋白的分子量为13438道尔顿。与谷物胰蛋白酶/α-淀粉酶抑制剂家族的其他成员一样，CM16蛋白含有10个半胱氨酸残基，其位置高度保守。在发育中的胚乳中，CM16 mRNA在成熟中期检测到最高水平。
