Suzuki T, Furukohri T
Department of Biology, Kochi University, Japan.
Experientia. 1989 Oct 15;45(10):998-1002. doi: 10.1007/BF01953061.
An unusual myoglobin was isolated from the buccal mass of the ear-shell Sulculus diversicolor aquatilis. The myoglobin consists of a 39 kDa polypeptide chain which is about double the size of the usual myoglobin subunit, contains one heme per molecule, and has an unusual spectral property ion the oxy-form. On the basis of these properties and partial amino acid sequencing, we propose that Sulculus myoglobin has a didomain structure, and that one of the two domains does not function as an oxygen-binding domain. So far, a myoglobin of this type has not been described in molluscs.
从耳贝多彩海牛的口腔团块中分离出一种不寻常的肌红蛋白。该肌红蛋白由一条39 kDa的多肽链组成，其大小约为普通肌红蛋白亚基的两倍，每个分子含有一个血红素，并且在氧合形式下具有不寻常的光谱特性。基于这些特性和部分氨基酸测序，我们提出多彩海牛肌红蛋白具有双结构域结构，并且两个结构域中的一个不作为氧结合结构域发挥作用。到目前为止，这种类型的肌红蛋白在软体动物中尚未见报道。
