Tanigawa M, Yamagami T, Funatsu G
Laboratory of Protein Chemistry & Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Biosci Biotechnol Biochem. 1995 May;59(5):841-7. doi: 10.1271/bbb.59.841.
The complete amino acid sequence of pokeweed leaf chitinase-B (PLC-B) has been determined by first sequencing all 19 tryptic peptides derived from the reduced and S-carboxymethylated (RCm-) PLC-B and then connecting them by analyzing the chymotryptic peptides from three fragments produced by cyanogen bromide cleavage of RCm-PLC-B. PLC-B consists of 274 amino acid residues and has a molecular mass of 29,473 Da. Six cysteine residues are linked by disulfide bonds between Cys20 and Cys67, Cys50 and Cys57, and Cys159 and Cys188. From 58-68% sequence homology of PLC-B with five class III chitinases, it was concluded that PLC-B is a basic class III chitinase.
商陆叶几丁质酶-B（PLC-B）的完整氨基酸序列已被确定。首先对还原和S-羧甲基化（RCm-）的PLC-B产生的所有19个胰蛋白酶肽段进行测序，然后通过分析溴化氰裂解RCm-PLC-B产生的三个片段中的胰凝乳蛋白酶肽段将它们连接起来。PLC-B由274个氨基酸残基组成，分子量为29473道尔顿。六个半胱氨酸残基通过Cys20和Cys67、Cys50和Cys57以及Cys159和Cys188之间的二硫键相连。根据PLC-B与五种III类几丁质酶58%-68%的序列同源性，得出PLC-B是一种碱性III类几丁质酶的结论。
