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J. Lipid Res.
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Originally published In Press as doi:10.1194/jlr.D900010-JLR200 on July 20, 2009

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Journal of Lipid Research, Vol. 51, 210-215, January 2010
Copyright © 2010 by American Society for Biochemistry and Molecular Biology

Methods

Adiponectin does not bind to gelatin: a new and easy way to purify high-molecular-weight adiponectin from human plasma

Yasuko Nakano1,*, Ayako Shoji*, Atsushi Arakawa*, Yumiko Iizuka*, Yuriko Kikuchi*, Maya Kobayashi* and Takashi Tobe{dagger}

* Department of Pharmacogenomics School of Pharmacy, Showa University, 1-5-8, Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan
{dagger} Center of Pharmaceutical Education, School of Pharmacy, Showa University, 1-5-8, Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan

1 To whom correspondence should be addressed. e-mail: yanakano{at}pharm.showa-u.ac.jp

Human plasma contains three forms of adiponectin, a trimer, a hexamer, and a high-molecular-weight (HMW) multimer. We previously reported HMW adiponectin was a gelatin-binding protein of 28 kDa (GBP28), it having been purified due to its affinity to gelatin-Cellulofine (Nakano, Y., et al. Isolation and characterization of GBP28, a novel gelatin-binding protein purified from human plasma. J. Biochem. 1996. 120: 803–12). Although HMW adiponectin binds to gelatin-Cellulofine, it cannot bind to gelatin-Sepharose. Gelatin-Cellulofine was made of formyl-Cellulofine and gelatin, and we found that HMW adiponectin binds to reduced formyl-Cellulofine with similar affinity as to gelatin-Cellulofine. Through only two steps using reduced formyl-Cellulofine and DEAE-Sepharose, HMW adiponectin can be effectively purified from human plasma.

Supplementary key words reduced formyl-Cellulofine • gelatin-Cellulofine • osteoclastogenesis


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