Purification and properties of lysyl- and methionyl-soluble ribonucleic acid synthetases from wheat germ

Esam Moustafa
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引用次数: 18

Abstract

Lysyl-s-RNA synthetase (l-lysine: s-RNA ligase (AMP), EC 6.1.1.6) and methionyl-s-RNA-synthetase (l-methionine: s-RNA ligase (AMP), EC 6.1.1.10) were purified from wheat germ about 600-fold and 160-fold, respectively. The two enzymes catalyse amino acid-dependent ATP-pyrophosphate exchange as well as the incorporation of amino acids into s-RNA. The pH optimum of lysine enzyme is in the range 6.8–7.1 and that of methionine enzyme in the range 8.1–8.5. Both enzymes are strongly inhibited by p-hydroxymercuribenzoate and the activity is restored by sulfhydryl group-containing compounds.

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小麦胚芽中赖氨酸和蛋氨酸可溶性核糖核酸合成酶的纯化及其性质
赖氨酸-s-RNA合成酶(l-赖氨酸:s-RNA连接酶(AMP), EC 6.1.1.6)和蛋氨酸-s-RNA合成酶(l-蛋氨酸:s-RNA连接酶(AMP), EC 6.1.1.10)从小麦胚芽中分别纯化了约600倍和160倍。这两种酶催化氨基酸依赖的atp -焦磷酸交换以及氨基酸与s-RNA的结合。赖氨酸酶的最适pH为6.8 ~ 7.1,蛋氨酸酶的最适pH为8.1 ~ 8.5。这两种酶都被对羟基氨基汞苯甲酸酯强烈抑制,并被含巯基的化合物恢复活性。
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Author index Erratum Subject index Changes in sedimentation properties of ribosomal ribonucleic acids during the course of ribosome formation in Escherichia coli The inhibition of deoxyribonucleotidyl transferase, DNAase and RNAase by sodium poly ethenesulfonic acid. Effect of the molecular weight of the inhibitor
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