Takagi T, Tobita M, Shikama K
Biochim Biophys Acta. 1983 May 30;745(1):32-6. doi: 10.1016/0167-4838(83)90166-8.
The complete amino acid sequence of the dimeric myoglobin from Cerithidea rhizophorarum, a common gastropodic mollusc on the Japanese coast having an elongated many-whorled shell, has been determined. The monomer is composed of 151 amino acid residues, is acetylated at the amino terminus, and 75 residues out of 151 are homologous with the monomer of myoglobin from the whelk Busycon canaliculatum. Unlike Aplysia myoglobin, which lacks the distal histidine, Cerithidea myoglobin contains three histidines in its monomer, His-66 being assigned to the distal position, and in its oxymyoglobin form its stability properties show a very strong pH dependence.
已确定采自日本海岸的一种常见腹足类软体动物——具有细长多旋壳的栖管蜒螺（Cerithidea rhizophorarum）的二聚体肌红蛋白的完整氨基酸序列。该单体由151个氨基酸残基组成，氨基末端被乙酰化，151个残基中有75个与蛾螺（Busycon canaliculatum）的肌红蛋白单体同源。与缺乏远端组氨酸的海兔肌红蛋白不同，栖管蜒螺肌红蛋白单体含有三个组氨酸，His-66位于远端位置，其氧合肌红蛋白形式的稳定性表现出很强的pH依赖性。
