Hayashi S, Nakamura S
Biochim Biophys Acta. 1981 Jan 15;657(1):40-51. doi: 10.1016/0005-2744(81)90128-5.
A glucose oxidase (beta-D-glucose:oxygen 1-oxidoreductase, EC 1.1.3.4) sample purified from Aspergillus niger by a previously reported method was subjected to isoelectric focusing and gel electrophoresis, and found to be composed of at least six component enzymes. The isoelectric points of the component enzymes ranged from pH 3.9 to 4.3. Analyses of the enzymes indicated that they all possess an identical protein moiety, since the amino acid compositions, the C-terminal sequences, the catalytic parameters, the quantitative and qualitative immunological properties and the electrophoretic patterns of the peptide fragments, obtained by the CNBr-cleavage, were practically the same. On the other hand, the carbohydrate contents of the isolated component enzymes were found to be different, and these differences were associated in the main with a particular peptide fragment. We suggest that the multiplicity of the enzyme is due to variation in the carbohydrate and their structures, rather than in the protein moiety.
采用先前报道的方法从黑曲霉中纯化得到的葡萄糖氧化酶（β-D-葡萄糖：氧1-氧化还原酶，EC 1.1.3.4）样品进行了等电聚焦和凝胶电泳，结果发现其至少由六种组分酶组成。这些组分酶的等电点范围为pH 3.9至4.3。对这些酶的分析表明，它们都具有相同的蛋白质部分，因为通过CNBr裂解获得的氨基酸组成、C末端序列、催化参数、定量和定性免疫特性以及肽片段的电泳图谱实际上是相同的。另一方面，发现分离得到的组分酶的碳水化合物含量不同，并且这些差异主要与一个特定的肽片段有关。我们认为该酶的多样性是由于碳水化合物及其结构的变化，而非蛋白质部分的变化。
