文献检索，用中文搜 PubMed

Suppr 超能文献

核心技术专利：CN118964589B侵权必究

核心技术专利：CN118964589B侵权必究

Kuwabara S, Lloyd P H

Biochem J. 1971 Aug;124(1):215-20. doi: 10.1042/bj1240215.

A crystalline preparation of beta-lactamase II has been separated into two moieties by gel filtration on a column of Sephadex G-100. 2. The first moiety consisted mainly of carbohydrate and showed virtually no beta-lactamase activity. 3. The second moiety was a protein of molecular weight 22500, which was enzymically active. 4. The protein moiety, like the original protein-carbohydrate complex, required Zn(2+) for beta-lactamase activity. It did not differ significantly from the complex in its behaviour to a number of cephalosporin substrates, but was less stable to heat than the complex. 5. About 30% of the total beta-lactamase activity was lost when the protein-carbohydrate complex was separated into the two moieties. This activity was regained when the protein and carbohydrate moieties were mixed, but the mixture did not show the heat stability of the original complex.

通过在葡聚糖凝胶G - 100柱上进行凝胶过滤，β - 内酰胺酶II的结晶制剂已被分离成两个部分。2. 第一部分主要由碳水化合物组成，几乎没有β - 内酰胺酶活性。3. 第二部分是一种分子量为22500的蛋白质，具有酶活性。4. 该蛋白质部分与原始的蛋白质 - 碳水化合物复合物一样，β - 内酰胺酶活性需要Zn(2+)。在对多种头孢菌素底物的反应中，它与复合物没有显著差异，但比复合物对热更不稳定。5. 当蛋白质 - 碳水化合物复合物被分离成两个部分时，总β - 内酰胺酶活性约损失30%。当蛋白质和碳水化合物部分混合时，这种活性得以恢复，但混合物没有显示出原始复合物的热稳定性。

Kuwabara S, Lloyd P H

Biochem J. 1971 Aug;124(1):215-20. doi: 10.1042/bj1240215.

A crystalline preparation of beta-lactamase II has been separated into two moieties by gel filtration on a column of Sephadex G-100. 2. The first moiety consisted mainly of carbohydrate and showed virtually no beta-lactamase activity. 3. The second moiety was a protein of molecular weight 22500, which was enzymically active. 4. The protein moiety, like the original protein-carbohydrate complex, required Zn(2+) for beta-lactamase activity. It did not differ significantly from the complex in its behaviour to a number of cephalosporin substrates, but was less stable to heat than the complex. 5. About 30% of the total beta-lactamase activity was lost when the protein-carbohydrate complex was separated into the two moieties. This activity was regained when the protein and carbohydrate moieties were mixed, but the mixture did not show the heat stability of the original complex.

通过在葡聚糖凝胶G - 100柱上进行凝胶过滤，β - 内酰胺酶II的结晶制剂已被分离成两个部分。2. 第一部分主要由碳水化合物组成，几乎没有β - 内酰胺酶活性。3. 第二部分是一种分子量为22500的蛋白质，具有酶活性。4. 该蛋白质部分与原始的蛋白质 - 碳水化合物复合物一样，β - 内酰胺酶活性需要Zn(2+)。在对多种头孢菌素底物的反应中，它与复合物没有显著差异，但比复合物对热更不稳定。5. 当蛋白质 - 碳水化合物复合物被分离成两个部分时，总β - 内酰胺酶活性约损失30%。当蛋白质和碳水化合物部分混合时，这种活性得以恢复，但混合物没有显示出原始复合物的热稳定性。