柿子果实β-半乳糖苷酶的N端氨基酸序列
N-terminal amino acid sequence of persimmon fruit beta-galactosidase.
作者信息
Kang I K, Suh S G, Gross K C, Byun J K
机构信息
Department of Horticulture, Yeungnam University, Kyongsan, Korea.
出版信息
Plant Physiol. 1994 Jul;105(3):975-9. doi: 10.1104/pp.105.3.975.
Abstract
beta-Galactosidase (EC 3.2.1.23) from persimmon fruit was purified 114-fold with a 15% yield using Sephadex G-100 gel filtration, CM-Sephadex ion exchange, and Sephacryl S-200 gel filtration chromatography, with subsequent electroelution from nondenaturing polyacrylamide gel electrophoresis (PAGE) gels. The estimated molecular mass of the native beta-galactosidase by Sephacryl S-200 was 118 kD. After sodium dodecyl sulfate-PAGE of the enzyme electroeluted from native gels, two subunits with estimated molecular masses of 34 and 44 kD were observed, suggesting that the native enzyme was an aggregate of several subunits. Amino acid composition and N-terminal amino acid sequences of the two major subunits were different.
摘要
利用葡聚糖凝胶G-100凝胶过滤、CM-葡聚糖离子交换和Sephacryl S-200凝胶过滤色谱法，从柿子果实中纯化β-半乳糖苷酶（EC 3.2.1.23），纯化倍数为114倍，产率为15%，随后通过非变性聚丙烯酰胺凝胶电泳（PAGE）凝胶进行电洗脱。通过Sephacryl S-200测定的天然β-半乳糖苷酶的估计分子量为118 kD。对从天然凝胶中电洗脱的酶进行十二烷基硫酸钠-PAGE后，观察到两个估计分子量分别为34 kD和44 kD的亚基，表明天然酶是几个亚基的聚集体。两个主要亚基的氨基酸组成和N端氨基酸序列不同。
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