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来自兔网织红细胞的脂氧合酶:铁含量、氨基酸组成及C末端异质性

Lipoxygenase from rabbit reticulocytes: iron content, amino acid composition and C-terminal heterogeneity.

作者信息

Wiesner R, Hausdorf G, Anton M, Rapoport S

出版信息

Biomed Biochim Acta. 1983;42(5):431-6.

PMID:6418154
Abstract

Purified lipoxygenase from rabbit reticulocytes contains 1 g atom iron per molecule. The amino acid composition shows that the enzyme contains 11 cysteine residues but no disulfide bridges and contains a relatively high content of hydrophobic amino acids. The enzyme shows heterogeneity in the C-terminus. With the tritium labeling method the amino acids His, Asn and Ile were found in the C-terminal region. The absorption co-efficient was found to be 1.68 (E0.1% 280 1 cm) in the native state and 1.77 in the unfolded state.

摘要

从兔网织红细胞中纯化得到的脂氧合酶,每个分子含有1克原子铁。氨基酸组成表明,该酶含有11个半胱氨酸残基,但没有二硫键,并且含有相对较高含量的疏水氨基酸。该酶在C末端表现出异质性。用氚标记法在C末端区域发现了组氨酸、天冬酰胺和异亮氨酸。在天然状态下,吸收系数为1.68(E0.1% 280 1厘米),在未折叠状态下为1.77。

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