Tumor Inhibitory and Non-Tumor Inhibitory l-Asparaginases from Pseudomonas geniculata

G. Barrie Kitto; Gale Smith; Tran-Quang Thiet; Mark Mason; Lois Davidson

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Tumor Inhibitory and Non-Tumor Inhibitory l-Asparaginases from Pseudomonas geniculata

机译：来自假单胞菌的肿瘤抑制和非肿瘤抑制l-天冬酰胺酶

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Two enzymes that catalyze the hydrolysis of l-asparagine have been isolated from extracts of Pseudomonas geniculata. After initial salt fractionation, the enzymes were separated by chromatography on diethylaminoethyl-Sephadex and purified to homogeneity by gel filtration, ion-exchange chromatography, and preparative polyacrylamide electrophoresis. The enzymes differ markedly in physicochemical properties. One enzyme, termed asparaginase A, has a molecular weight of approximately 96,000 whereas the other, termed asparaginase AG, has a molecular weight of approximately 135,000. Both enzymes are tetrameric. The asparaginase A shows activity only with l-asparagine as substrate, whereas the asparaginase AG hydrolyzes l-asparagine and l-glutamine at approximately equal rates and it is also active with d-asparagine and d-glutamine as substrates. The asparaginase A was found to be devoid of antitumor activity in mice, whereas the asparaginase AG was effective in increasing the mean survival times of both C3H mice carrying the asparagine-requiring Gardner 6C3HED tumor line and Swiss mice bearing the glutamine-requiring Ehrlich ascites tumor line. These differences in antitumor activity were related to differences in the K_m values for l-asparagine for the two enzymes. The asparaginase A has a K_m value of 1 × 10?3 M for this substrate whereas the corresponding value for the AG enzyme is 1.5 × 10?5 M. Thus the concentration of asparagine necessary for maximal activity of the asparaginase A is very high compared with that of the normal plasma level of asparagine, which is approximately 50 μM.

机译：催化L-天冬酰胺水解的两种酶已从假单胞菌Geniculata提取物中分离出来。初始盐分馏后，通过凝胶过滤，离子交换色谱和制备聚丙烯酰胺电泳纯化酶。通过凝胶过滤，离子交换色谱法和制备聚丙烯酰胺电泳纯化，纯化至均匀性。酶在物理化学性质中显着不同。一种称为天冬酰胺酶A的一种酶，其分子量约为96,000，而另一个称为天冬酰胺酶Ag的分子量约为135,000。两种酶都是四聚体。天冬酰胺酶A显示仅含有L-天冬酰胺作为底物的活性，而浅氨氨基酶Ag以大致相等的速率水解L-天冬酰胺和L-谷氨酸，并且还与D-天冬酰胺和D-谷氨酰胺作为基质有活性。发现天冬酰胺酶A缺乏小鼠的抗肿瘤活性，而芦巴蛋白酶Ag是有效地增加携带天冬酰胺的C3H小鼠的平均存活时间，载冬酰胺的加德纳6c3hed肿瘤系和携带谷氨酰胺的ehrlich腹水肿瘤的瑞士小鼠线。抗肿瘤活性的这些差异与用于两种酶的L-天冬酰胺的 K _{m 值的差异有关。天冬酰胺酶A具有1×10 α3/ em>值的 k _{m m。对于该基板，而Ag酶的相应值是1.5×因此，与天冬酰胺的正常血浆水平相比，10 α5 5。与天冬酰胺的正常血浆水平相比，浅冬蛋白酶A的最大活性所需的浓度非常高。}} 展开▼

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《Journal of bacteriology》 |1979年第1期|共9页

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G. Barrie Kitto; Gale Smith; Tran-Quang Thiet; Mark Mason; Lois Davidson;
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1. Tumor Inhibitory and Non-Tumor Inhibitory l-Asparaginases from Pseudomonas geniculata [J] . G. Barrie Kitto, Gale Smith, Tran-Quang Thiet, Journal of bacteriology . 1979,第1期

机译：来自假单胞菌的肿瘤抑制和非肿瘤抑制l-天冬酰胺酶

2. Tumor Inhibitory and Non-Tumor Inhibitory l-Asparaginases from Pseudomonas geniculata [J] . G. Barrie Kitto, Gale Smith, Tran-Quang Thiet, Journal of bacteriology . 1979,第1期

机译：来自假单胞菌的肿瘤抑制和非肿瘤抑制l-天冬酰胺酶

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6. Tumor Inhibitory and Non-Tumor Inhibitory l-Asparaginases from Pseudomonas geniculata [O] . G. Barrie Kitto, Gale Smith, Tran-Quang Thiet, 1979

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Tumor Inhibitory and Non-Tumor Inhibitory l-Asparaginases from Pseudomonas geniculata

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