Sakurada M, Morgavi D P, Ushirone N, Komatani K, Tomita Y, Onodera R
Laboratory of Animal Nutrition and Biochemistry, Faculty of Agriculture, Miyazaki University, Miyazaki 889-21, Japan.
Curr Microbiol. 1998 Jul;37(1):60-3. doi: 10.1007/s002849900338.
A membrane-bound chitinase from cell wall fractions of the anaerobic ruminal fungus, Piromyces communis OTS1, was purified by affinity chromatography, gel filtration, and chromatofocusing. The molecular size of the chitinase was estimated by gel filtration to be 42.4 kDa and by SDS-PAGE to be 44.8 kDa, and its pI was 4.4. Activity was inhibited by Hg2+ and allosamidin. The activity at 39 degrees C was greatest at pH 6.0. It had an 'endo' type action. Solubilization tests indicated that plasmalemma-bound chitinase was held in place by an electrostatic type interaction. Characterization of the membrane-bound chitinase was more similar to that of extracellular chitinase than cytosolic chitinase. This suggested that membrane-bound chitinase was the origin of extracellular chitinase.
通过亲和色谱法、凝胶过滤法和色谱聚焦法，从厌氧瘤胃真菌普通梨形菌OTS1的细胞壁组分中纯化出一种膜结合几丁质酶。通过凝胶过滤法估计该几丁质酶的分子大小为42.4 kDa，通过SDS-PAGE法估计为44.8 kDa，其pI为4.4。Hg2+和别洛沙米定抑制其活性。在39摄氏度时，pH 6.0时活性最高。它具有“内切”型作用。增溶试验表明，质膜结合的几丁质酶通过静电型相互作用固定在原位。膜结合几丁质酶的特性与细胞外几丁质酶的特性比细胞溶质几丁质酶的特性更相似。这表明膜结合几丁质酶是细胞外几丁质酶的来源。
