Subunits of Panulirus japonicus hemocyanin
Subunits of Panulirus japonicus hemocyanin
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日本龙虾血蓝蛋白亚基
DOI：
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发表时间：
1988
期刊：
影响因子：
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通讯作者：
S. Kimura
中科院分区：
文献类型：
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作者：
N. Makino;S. Kimura
对龙虾血蓝蛋白亚基的结构和功能进行了研究。血蓝蛋白在天然状态下主要以六聚体形式存在。结果表明，血蓝蛋白由三个主要亚基（Ib，II和III）和一个次要亚基（Ia）组成，它们的N-末端序列不同。在解离状态下，主要亚基（Ib，II和III）没有或非常小的玻尔效应。亚基III的O2亲和力约为其他两个亚基的3倍。
这些亚基可以重新结合成同质和异质的六聚体，它们在O2结合中表现出协同性。的homohexamers是彼此相似的O2亲和力和玻尔效应，虽然观察到一些差异的协同性的大小。特别是，亚基II homohexamer表现出很高的协同性，这是可比的天然蛋白质。的heterohexamers表现出略高的O2亲和力和略低的cooperativity，与父母homohexamers相比。
结果表明，血蓝蛋白的三个主要亚基在O2结合和组装特性上没有本质差异。
Structural and functional diversities of the subunits of Panulirus japonicus (spiny lobster) hemocyanin were investigated. The hemocyanin mostly exists as a hexamer in the native state. It was found that the hemocyanin is composed of three major subunits (Ib, II and III) and one minor subunit (Ia), which differ in N-terminal sequence. In the dissociated state, the major subunits (Ib, II and III) showed no or very small Bohr effects. The O2 affinity of the subunit III was about three times as high as those of the other two.
The subunits could be reassociated into homogeneous and heterogeneous hexamers, which exhibited the cooperativity in O2 binding. The homohexamers were similar to each other in O2 affinity and the Bohr effect, though some differences were observed in the magnitude of the cooperativity. In particular, the subunit II homohexamer exhibited a high cooperativity, which was comparable to that of the native protein. The heterohexamers showed slightly higher O2 affinities and slightly lower cooperativity, as compared with the parent homohexamers.
It was concluded that there is no essential difference among the three major subunits of P. japonicus hemocyanin in the O2 binding and assembly properties.
通过分子免疫电子显微镜用单克隆抗体直接分子内定位Androctonus australis血蓝蛋白中的抗原决定簇。
影响因子：
2.9
作者：
Lamy,J;Lamy,J;Billiald,P;Sizaret,PY;Cavé,G;Frank,J;Motta,G
通讯作者：
Motta,G