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Keyhole limpet hemocyanin : ウィキペディア英語版 | Keyhole limpet hemocyanin
Keyhole limpet hemocyanin (KLH) is a large, multisubunit, oxygen-carrying, metalloprotein that is found in the hemolymph of the giant keyhole limpet, ''Megathura crenulata'', a species of keyhole limpet that lives off the coast of California, from Monterey Bay to Isla Asuncion off Baja California. ==Protein properties== There are two keyhole limpet hemocyanin genes, termed KLH1 and KLH2 which share around 60% identity at the protein level. Both encode large glycosylated proteins consisting of around 3400 amino acids and a molecular weight of around 390,000 Daltons, excluding the glycosylation. The protein oligomerises to form a barrel shaped didecameric complex which is composed of 20 monomers. Each domain of a KLH subunit contains two copper atoms that together bind a single oxygen molecule (O2). When oxygen is bound to hemocyanin, the molecule takes on a distinctive transparent, opalescent blue color, due to the Cu2+ state of the copper. In the absence of oxygen, the bound copper is found as Cu1+ and hemocyanin is colorless. The KLH protein is potently immunogenic, but does not cause an adverse immune response in humans. It is therefore highly prized as a vaccine carrier protein. Because of its size and glycosylation, KLH protein cannot be reproduced synthetically; it is available only as a purified biological product from the keyhole limpet ''Megathura crenulata''.
抄文引用元・出典: フリー百科事典『 ウィキペディア(Wikipedia)』 ■ウィキペディアで「Keyhole limpet hemocyanin」の詳細全文を読む
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