The cDNA-derived amino acid sequence of indoleamine dioxygenase like-myoglobin from the gastropod mollusc Omphalius pfeifferi
The cDNA-derived amino acid sequence of indoleamine dioxygenase like-myoglobin from the gastropod mollusc Omphalius pfeifferi
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DOI：
10.1007/bf02780966
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发表时间：
1998-10-01
期刊：
影响因子：
--
通讯作者：
Suzuki, T
中科院分区：
文献类型：
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作者：
Kawamichi, K;Suzuki, T
肌红蛋白是从古腹足类软体动物 Omphalius pfeifferi（Trochidae）的齿根肌中分离出来的。 SDS-PAGE估计其分子量约为40 kDa，是普通肌红蛋白的2.5倍。通过聚合酶链式反应扩增了Omphalius肌红蛋白的cDNA，并确定了cDNA衍生的375个残基的氨基酸序列，其中73个残基通过内肽化学测序直接鉴定。 Omphalius 肌红蛋白的氨基酸序列与任何其他常见的 16 kDa 球蛋白没有显着同源性，但与来自 Battilus (Turbinidae) 和 Sulculus (Haliotiidae) 的吲哚胺双加氧酶样肌红蛋白分别有 84% 和 36% 的同一性。它还与人吲哚胺 2,3-双加氧酶（一种含有血红素的色氨酸降解酶）显示出显着的同源性（26% 同一性）。吲哚胺双加氧酶样肌红蛋白的分布表明，它们一定是沿着软体动物进化中的特定谱系专门产生的，包括古腹足纲的鲍科、鳐科和特罗奇科三个科。
Myoglobin was isolated from the radular muscle of the archaegastropod mollusc Omphalius pfeifferi (Trochidae). The molecular mass was estimated by SDS-PAGE to be about 40 kDa, 2.5 times larger than that of usual myoglobin. The cDNA for Omphalius myoglobin was amplified by polymerase chain reaction, and the cDNA-derived amino acid sequence of 375 residues was determined, of which 73 residues were identified directly by the chemical sequencing of internal peptides. The amino acid sequence of Omphalius myoglobin showed no significant homology with any other usual 16-kDa globins, but showed 84% and 36% identities with indoleamine dioxygenase-like myoglobins from Battilus (Turbinidae) and Sulculus (Haliotiidae), respectively. It also shows significant homology (26% identity) with human indoleamine 2,3-dioxygenase, a tryptophan-degrading enzyme containing heme. The distribution of indoleamine dioxygenase-like myoglobins suggests that they must have arisen exclusively along the specified lineage including the three families Haliotiidae, Turbinidae, and Trochidae of Archaegastropoda in molluscan evolution.