Mauri F, Omnaas J, Davidson L, Whitfill C, Kitto G B
Clayton Foundation Biochemical Institute, Department of Chemistry and Biochemistry, University of Texas, Austin.
Biochim Biophys Acta. 1991 May 30;1078(1):63-7. doi: 10.1016/0167-4838(91)90093-f.
Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major globins, A, B, C and D. The hemoglobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate globins. The C. arenicola D globin has an equal sequence identity (28%) with both alpha and beta human globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan globins. The C. arenicola D globin shows a 59% identity with the globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.
海黄瓜（Caudina (Molpadia) arenicola）的体腔细胞含有四种主要的球蛋白，A、B、C和D。该生物体的血红蛋白表现出不同寻常的配体连接解离特性。D球蛋白的完整氨基酸序列已确定。它是N-乙酰化的，由158个残基组成，并且有一个10个氨基酸的N端延伸，类似于在其他一些无脊椎动物球蛋白中发现的延伸。C. arenicola D球蛋白与人类α和β球蛋白具有相同的序列同一性（28%），并且正如预期的那样，与这些脊椎动物蛋白质的关系比软体动物球蛋白更密切。C. arenicola D球蛋白与海参Paracaudina chilensis的球蛋白I具有59%的同一性。C. arenicola D球蛋白序列的可得性将有助于对该蛋白质进行X射线分析，并促进对协同配体结合时亚基相互作用变化的理解。
Zotero 插件