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

作者：Nakano Yasuko^*; Shoji Ayako; Arakawa Atsushi; Iizuka Yumiko; Kikuchi Yuriko; Kobayashi Maya; Tobe Takashi

来源：The Journal of Lipid Research, 2010, 51(1): 210-215.

DOI：10.1194/jlr.D900010-JLR200

• reduced formyl-Cellulofine
• gelatin-Cellulofine
• osteoclastogenesis

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.-Nakano, Y., A. Shoji, A. Arakawa, Y. Iizuka, Y. Kikuchi, M. Kobayashi, and T. Tobe. Adiponectin does not bind to gelatin: a new and easy way to purify high-molecular-weight adiponectin from human plasma. J. Lipid Res. 2010. 51: 210-215.

• 出版日期2010-1