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. Structured summary of protein interactionsLECT2 and LECT2bind by cross-linking study (View interaction)LECT2 and LECT2bind by comigration in gel electrophoresis (View interaction)LECT2 and LECT2bind by comigration in gel electrophoresis (View interaction: 1, 2, 3)LECT2 and LECT2bind by cross-linking study (View interaction: 1, 2, 3)LECT2 and LECT2bind by comigration in gel electrophoresis (View interaction: 1, 2, 3)
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