| Literature DB >> 23352894 |
Akinori Okumura1, Takehiro Suzuki, Hideyuki Miyatake, Tomoya Okabe, Yuki Hashimoto, Takuya Miyakawa, Hai Zheng, Hiroyuki Unoki-Kubota, Hideaki Ohno, Naoshi Dohmae, Yasushi Kaburagi, Yoshitsugu Miyazaki, Masaru Tanokura, Satoshi Yamagoe.
Abstract
Leukocyte cell-derived chemotaxin 2 (LECT2) is a secreted hepatic protein that has been associated with several physiological activities. LECT2 belongs to the peptidase M23 family, suggesting that it is a zinc-binding protein. To test this possibility, electrospray ionization mass spectrometry and X-ray absorption fine-structure analysis were performed. Results of these experiments indicated that recombinant mouse LECT2 produced by an animal cell line contains a zinc atom. Furthermore, the recombinant LECT2 was found to be self-oligomerized by disulfide bonds in vitro, but this was suppressed by addition of zinc. These results indicated that zinc stabilizes the LECT2 structure.Entities:
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Year: 2013 PMID： 23352894 DOI： 10.1016/j.febslet.2013.01.025
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124