MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it The proline-rich tetramerization peptides in equine serum butyrylcholinesterase. The proline-rich tetramerization peptides in equine serum butyrylcholinesterase. FEBS J. (1742-464X) 2012 Biberoglu K., Schopfer LM., Tacal O., Lockridge O. in vitro In vitro comig non denat gel comigration in non denaturing gel electrophoresis comig non denat gel predetermined predetermined participant predetermined Biberoglu K., Schopfer LM., Tacal O., Lockridge O. FEBS J. (1742-464X) 2012 The proline-rich tetramerization peptides in equine serum butyrylcholinesterase. The proline-rich tetramerization peptides in equine serum butyrylcholinesterase. FEBS J. (1742-464X) 2012 Biberoglu K., Schopfer LM., Tacal O., Lockridge O. in vitro In vitro comigration in sds comigration in sds page comigration in sds predetermined predetermined participant predetermined Biberoglu K., Schopfer LM., Tacal O., Lockridge O. FEBS J. (1742-464X) 2012 q9n1n9_horse Carboxylic ester hydrolase BCHE protein protein horse Equus caballus (Horse) Horse MQSWGTIICIRILLRFLLLWVLIGNSHTEEDIIITTKNGKVRGMNLPVLGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSNIWNATKYANSCYQNTDQSFPGFLGSEMWNPNTELSEDCLYLNVWIPAPKPKNATVMIWIYGGGFQTGTSSLPVYDGKFLARVERVIVVSMNYRVGALGFLALSENPEAPGNMGLFDQQLALQWVQKNIAAFGGNPRSVTLFGESAGAASVSLHLLSPRSQPLFTRAILQSGSSNAPWAVTSLYEARNRTLTLAKRMGCSRDNETEMIKCLRDKDPQEILLNEVFVVPYDTLLSVNFGPTVDGDFLTDMPDTLLQLGQFKRTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPRVSEFGRESILFHYMDWLDDQRAENYREALDDVVGDYNIICPALEFTKKFSELGNDAFFYYFEHRSTKLPWPEWMGVMHGYEIEFVFGLPLERRVNYTKAEEILSRSIMKRWANFAKYGNPNGTQSNSTRWPVFKSTEQKYLTLNTESPKVYTKLRAQQCRFWTLFFPKVLELTGNIDEAEREWKAGFHRWNNYMMDWKNQFNDYTSKKESCSDF mint 94C73F00431DF26E bche-1 1 BChE 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 4.0 direct interaction direct interaction f6 mint Coomassie blue staining of purified horse BChE on a nondenaturing gel showed that the position of tetrameric horse BChE (not boiled, lane 5) was identical to the tetrameric BChE band in the gel stained for BChE activity (lane 3). Unexpectedly, the boiled form of horse BChE traveled at a position between tetramer and dimer, roughly at the position expected for a trimer (lane 6). Shape is an important determinant of migration on non-denaturing gels. We suggest that the boiled horse BChE dissociates into dimers and then rearranges to form aggregates such that normal dimeric migration of BChE is not seen. bche-1 2 BChE 3 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified Stoichiometry: 2.0 direct interaction direct interaction f7 mint To further examine the quaternary structure of horse BChE we performed SDSPAGE in the presence and absence of dithiothreitol. Figure 7 shows that in the absence of dithiothreitol denatured horse BChE migrates primarily as a dimer (lane 1). Boiling did not change this pattern (lane 2) indicating that boiling did not cause fragmentation of the subunits. Addition of dithiothreitol followed by boiling caused the majority of the BChE to be converted into monomers (lane 3). Thus, like human BChE, tetrameric horse BChE consists of a dimer of cysteine cross-linked dimers.