PURIFICATION AND CHARACTERIZATION OF 2 CHITINASES FROM THE LEAVES OF POKEWEED (PHYTOLACCA-AMERICANA)

被引：26

作者：

OHTA, M ^{[1
]}

YAMAGAMI, T ^{[1
]}

FUNATSU, G ^{[1
]}

机构：

[1] KYUSHU UNIV, FAC AGR, PROT CHEM & ENGN LAB, FUKUOKA 812, JAPAN

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 1995年 / 59卷 / 04期

关键词：

D O I：

10.1271/bbb.59.656

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Two chitinases, designated PLC-A and PLC-B, were purified from the leaves of pokeweed (Phytolacca americana) using DEAE-cellulose column chromatography followed by gel filtration on Sephadex G-75, hydrophobic column chromatography, and ion-exchange FPLC., PLC-A and PLC-B are acidic and basic proteins having molecular masses of 25 and 29 kDa, and isoelectric points of 3.7 and 9.5, respectively, On the basis of their partial amino acid sequences, it was seen that PLC-A and PLC-B belong to class II and class III chitinases, respectively, The optimal pH of PLC-A toward glycolchitin is pH 4.5 and hydrolyzed (GlcNAc)(4) into 2(GlcNAc)(2), and (GlcNAc)(5-6) into (GlcNAc)(2) and (GlcNAc)(3). On the other hand, PLC-B has two optimal pi-Is at 3 and 7 toward glycolchitin and hydrolyzed (GlcNAc)(5) into GlcNAc and (GlcNAc)(4), and (GlcNAc)(6) into GlcNAc, (GlcNAc)(2), and (GlcNAc)(4).

引用

页码：656 / 661

页数：6

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