首页> 外文期刊>Toxicon: An International Journal Devoted to the Exchange of Knowledge on the Poisons Derived from Animals, Plants and Microorganisms >CLONING AND CHARACTERIZATION OF THE CDNAS ENCODING NA+ CHANNEL-SPECIFIC TOXINS 1 AND 2 OF THE SCORPION CENTRUROIDES NOXIUS HOFFMANN
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CLONING AND CHARACTERIZATION OF THE CDNAS ENCODING NA+ CHANNEL-SPECIFIC TOXINS 1 AND 2 OF THE SCORPION CENTRUROIDES NOXIUS HOFFMANN

机译:CDNAS的克隆和表征,包括蝎COR中的NA +通道特异性毒素1和2。

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Using a cDNA library prepared from venomous glands of the Mexican scorpion Centruroides noxius Hoffmann the genes that encode toxins 1 and 2 were identified, cloned and sequenced. In view of the proposed mechanism for processing the mature peptides coded by these two genes, the corresponding peptide-toxins were sequenced de novo. Mass spectrometric and H-1-NMR analyses of the C-terminal peptide produced by enzymatic digestion of both toxins indicated that the last residue is serine-amide. Sequence comparison revealed that these two genes have a similarity of 56% and 80% at the amino acid and nucleotide levels, respectively. Small corrections to the published primary structures were introduced: Cn toxin 1 has an extra serine residue at position 65 and the residue in position 60 is a proline, while the amino acids at positions 34 and 35 of Cn 2 are, respectively, tyrosine and glycine. Sequence comparison of toxins from the genus Centruroides suggests the presence of at least three classes of distinct peptides in these venoms. [References: 28]
机译:使用从墨西哥蝎形夜蛾霍夫曼毒液腺制备的cDNA文库,鉴定,克隆和测序了编码毒素1和2的基因。鉴于提出的加工这两个基因编码的成熟肽的机制,从头对相应的肽毒素进行了测序。两种毒素的酶消化产生的C端肽的质谱和H-1-NMR分析表明,最后一个残基是丝氨酸酰胺。序列比较显示这两个基因在氨基酸和核苷酸水平上的相似性分别为56%和80%。对已发表的一级结构进行了一些小的修正:Cn毒素1在65位具有一个额外的丝氨酸残基,而60位则为脯氨酸,而Cn 2的34位和35位氨基酸分别为酪氨酸和甘氨酸。 。来自Centurouroides属的毒素的序列比较表明,在这些毒液中至少存在三类不同的肽。 [参考:28]

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