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Identification of lysine (384) in cytochrome P-450 LM2 as functionally linked residue.

作者信息

Makower A, Bernhardt R, Rabe H, Jänig G R, Ruckpaul K

出版信息

Biomed Biochim Acta. 1984;43(12):1333-41.

PMID:6442864
Abstract

Fluorescein isothiocyanate was selectively bound to the epsilon-amino group of a lysine residue of cytochrome P-450 LM2 at rho H 8.15. The decrease in the N-demethylase activity after modification evidences the functional importance of the modified group. After tryptic digestion the FITC-labeled peptide was isolated by means of HPLC and its amino acid composition determined. It was shown that the FITC-peptide can be attributed to the sequence Gly (379)- Arg (400) and that the label is selectively bound to Lys (384).

摘要

相似文献

1
Identification of lysine (384) in cytochrome P-450 LM2 as functionally linked residue.
Biomed Biochim Acta. 1984;43(12):1333-41.
2
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3
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Selective chemical modification of a functionally linked lysine in cytochrome P-450 LM2.细胞色素P-450 LM2中功能连接赖氨酸的选择性化学修饰。
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Distance between lysine 384 and heme of cytochrome P-450 LM2 (P-450 IIB4) studied by fluorescence energy transfer measurements.
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7
Modification of cytochrome P-450 with fluorescein isothiocyanate.
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9
"Lysine is the Lord", thought some scientists in regard to the group interacting with fluorescein isothiocyanate in ATP-binding sites of P-type ATPases but, is it not cysteine?一些科学家认为在P型ATP酶的ATP结合位点中与异硫氰酸荧光素相互作用的基团是赖氨酸，但是，难道不是半胱氨酸吗？
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