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磷脂酶C(蜡样芽孢杆菌)中明显必需赖氨酸残基的鉴定

Identification of the apparently essential lysine residues in phospholipase C (Bacillus cereus).

作者信息

Myrnes B J, Little C

出版信息

Biochem J. 1981 Mar 1;193(3):805-9. doi: 10.1042/bj1930805.

Abstract

Phospholipase C (Bacillus cereus) contains two apparently essential and very reactive lysine residues that may be labelled selectively by pyridoxal 5'-phosphate [Aurebekk & Little (1977) Biochem, J. 161, 159--165]. One of these lysine residues was found in the 25-amino acid N-terminal fragment liberated by CNBr digestion of the pyridoxal-labelled enzyme and identified as lysine-6. Two of the labelled peptides isolated from the chymotryptic digest of pyridoxal-labelled enzyme contained proline, suggesting that the other labelled lysine residue is situated in the same region of the primary structure as the single proline residue of the enzyme.

摘要

磷脂酶C(蜡样芽孢杆菌)含有两个明显必需且反应性很强的赖氨酸残基,它们可能被磷酸吡哆醛选择性标记[Aurebekk和Little(1977年),《生物化学杂志》,161卷,第159 - 165页]。通过对磷酸吡哆醛标记的酶进行溴化氰消化释放出的25个氨基酸的N端片段中发现了其中一个赖氨酸残基,并鉴定为赖氨酸 - 6。从磷酸吡哆醛标记的酶的胰凝乳蛋白酶消化物中分离出的两个标记肽含有脯氨酸,这表明另一个标记的赖氨酸残基位于该酶的单个脯氨酸残基所在的一级结构区域。

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本文引用的文献

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Biochem J. 1970 Oct;119(5):805-22. doi: 10.1042/bj1190805f.
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The metal ion dependence of phospholipase C from Bacillus cereus.蜡样芽孢杆菌磷脂酶C的金属离子依赖性
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