Binding of murine monoclonal antibodies to the active and inactive configurations of aequorin

FEBS Letters

Kurihara, Satoshi²  Inouye, Satoshi³  Ohno, Tsuneya¹  Watanabe, Michiko¹ 

[1] 1st Department of Microbiology, The Jikei University School of Medicine, 3-25-8 Nishi-shinbashi, Minato-ku, Tokyo 105, Japan;2nd Department of Physiology, The Jikei University School of Medicine, 3-25-8 Nishi-shinbashi, Minato-ku, Tokyo 105, Japan;Basic Research Laboratories Corporate Technical Division, Chisso Corporation, 2 Kamariya, Kanazawa-ku, Yokohama 236, Japan

关键词: Aequorin;    Monoclonal antibody;    Active form;    Inactive form;   

DOI  :  10.1016/0014-5793(89)80256-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Murine monoclonal IgG₁ antibodies (MAb), designated Aq-11 and Aq-12, were prepared against the photoprotein aequorin from jelly fish. Aequorin is a calcium-sensitive photoprotein which consists of a single polypeptide chain, apoaequorin, and a functional chromophore, coelenterazine. Native aequorin consists of two species with molecular masses of 25 and 23.5 kDa. MAb Aq-12 was found by immunoblot analysis to bind specifically to the 25 kDa species, while MAb Aq-11 reacted with the 23.5 kDa protein. Activation of apoaequorin with coelenterazine was associated with a shift of the 23.5 kDa molecule to the 25 kDa species. In contrast, treatment with calcium ions induced a shift back to the 23.5 kDa form. These changes between the active and inactive forms were identified by reactivity with MAbs Aq-11 and Aq-12. The results thus indicate that these MAbs should be useful in monitoring activation of this photoprotein.

【 授权许可】

Unknown