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[来自苍白曲霉的核糖核酸酶Ap1。纯化、一级结构及结晶]

[Ribonuclease Ap1 from Aspergillus pallidus. Purification, primary structure and crystallization].

作者信息

Bezborodova S I, Ermekbaeva L A, Shliapnikov S V, Poliakov K M, Bezborodov A M

出版信息

Biokhimiia. 1988 Jun;53(6):965-73.

PMID:3140903
Abstract

Extracellular guanyl-specific RNAase of the fungus Aspergillus pallidus (RNAase ApI) was isolated in preparative amounts with a 40% yield and purified to homogeneity (938-fold). The complete amino acid sequence of the protein (104 amino acid residues) was determined: 6 Asp, 4 Asn, 4 Thr, 14 Ser, 3 Glu, 4 Gln, 4 Pro, 15 Gly, 9 Ala, 4 Cys, 6 Val, 2 Ile, 4 Leu, 10 Tyr, 4 Phe, 3 His, 4 Arg, 1 Trp. RNAase ApI has a molecular mass of 11,029 Da and is homologous to the family of fungal extracellular guanyl-specific RNAases. The primary structure of the protein is close to that of RNAase C2 from Asp. clavatus and differs from it by only 4 substitutions of amino acid residues. Monocrystals of RNAase ApI were grown which can be used for the X-ray analysis of proteins.

摘要

从苍白曲霉(RNA酶ApI)中分离出了制备量的细胞外鸟苷特异性RNA酶,产率为40%,并纯化至同质(938倍)。确定了该蛋白质的完整氨基酸序列(104个氨基酸残基):6个天冬氨酸、4个天冬酰胺、4个苏氨酸、14个丝氨酸、3个谷氨酸、4个谷氨酰胺、4个脯氨酸、15个甘氨酸、9个丙氨酸、4个半胱氨酸、6个缬氨酸、2个异亮氨酸、4个亮氨酸、10个酪氨酸、4个苯丙氨酸、3个组氨酸、4个精氨酸、1个色氨酸。RNA酶ApI的分子量为11,029道尔顿,与真菌细胞外鸟苷特异性RNA酶家族同源。该蛋白质的一级结构与棒曲霉的RNA酶C2接近,仅在4个氨基酸残基取代上与之不同。培养出了RNA酶ApI的单晶,可用于蛋白质的X射线分析。

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