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核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Nicholas P C, Bachelard H S

Biochem J. 1969 May;112(5):587-94. doi: 10.1042/bj1120587.

Aldolase isoenzymes from guinea-pig cerebral cortex were partially purified and separated by ammonium sulphate fractionation and chromatography on DEAE-cellulose. 2. Each purified isoenzyme was shown to be virtually uncontaminated with other forms by starch-gel electrophoresis. The quantitative distribution of the isoenzymes was: I, 6.2%; II, 5.2%; III, 15.3%; IV, 25.7%; V, 33.3%. 3. The pH optima for the five separated isoenzymes were similar; all were in the range pH7.5-8.0. Values for pK(a) (6.31-6.55) and pK(b) (9.45-9.59) were calculated from the data and suggested the involvement of histidine and lysine residues. 4. The stabilities of the isoenzymes were shown to be I=II>III>IV>V at pH4.4 in order of decreasing stability and are discussed in terms of subunit structure. 5. The substrate activity ratios (fructose 1,6-diphosphate/fructose 1-phosphate) were measured and all were in the range 12-44.

对豚鼠大脑皮层的醛缩酶同工酶进行了部分纯化，并通过硫酸铵分级分离和DEAE - 纤维素柱色谱法进行分离。2. 通过淀粉凝胶电泳表明，每种纯化的同工酶几乎未被其他形式污染。同工酶的定量分布为：I，6.2%；II，5.2%；III，15.3%；IV，25.7%；V，33.3%。3. 分离出的五种同工酶的最适pH值相似；均在pH7.5 - 8.0范围内。根据数据计算出pK(a)（6.31 - 6.55）和pK(b)（9.45 - 9.59）的值，表明组氨酸和赖氨酸残基参与其中。4. 在pH4.4条件下，同工酶的稳定性表现为I = II>III>IV>V，稳定性依次降低，并根据亚基结构进行了讨论。5. 测量了底物活性比（果糖1,6 - 二磷酸/果糖1 - 磷酸），所有比值均在12 - 44范围内。

Nicholas P C, Bachelard H S

Biochem J. 1969 May;112(5):587-94. doi: 10.1042/bj1120587.

Aldolase isoenzymes from guinea-pig cerebral cortex were partially purified and separated by ammonium sulphate fractionation and chromatography on DEAE-cellulose. 2. Each purified isoenzyme was shown to be virtually uncontaminated with other forms by starch-gel electrophoresis. The quantitative distribution of the isoenzymes was: I, 6.2%; II, 5.2%; III, 15.3%; IV, 25.7%; V, 33.3%. 3. The pH optima for the five separated isoenzymes were similar; all were in the range pH7.5-8.0. Values for pK(a) (6.31-6.55) and pK(b) (9.45-9.59) were calculated from the data and suggested the involvement of histidine and lysine residues. 4. The stabilities of the isoenzymes were shown to be I=II>III>IV>V at pH4.4 in order of decreasing stability and are discussed in terms of subunit structure. 5. The substrate activity ratios (fructose 1,6-diphosphate/fructose 1-phosphate) were measured and all were in the range 12-44.

对豚鼠大脑皮层的醛缩酶同工酶进行了部分纯化，并通过硫酸铵分级分离和DEAE - 纤维素柱色谱法进行分离。2. 通过淀粉凝胶电泳表明，每种纯化的同工酶几乎未被其他形式污染。同工酶的定量分布为：I，6.2%；II，5.2%；III，15.3%；IV，25.7%；V，33.3%。3. 分离出的五种同工酶的最适pH值相似；均在pH7.5 - 8.0范围内。根据数据计算出pK(a)（6.31 - 6.55）和pK(b)（9.45 - 9.59）的值，表明组氨酸和赖氨酸残基参与其中。4. 在pH4.4条件下，同工酶的稳定性表现为I = II>III>IV>V，稳定性依次降低，并根据亚基结构进行了讨论。5. 测量了底物活性比（果糖1,6 - 二磷酸/果糖1 - 磷酸），所有比值均在12 - 44范围内。