Waugh, Stephen M. published the artcileIsolation of a proteolytically derived domain of the insulin receptor containing the major site of cross-linking/binding, Category: alcohols-buliding-blocks, the publication is Biochemistry (1989), 28(8), 3448-55, database is CAplus and MEDLINE.
Radiolabeled insulin was affinity crosslinked to purified insulin receptor with 6 sep. bifunctional N-hydroxysuccinimde esters of different lengths. Results were qual. identical for each crosslinker in that insulin was predominantly crosslinked through its B chain to the receptor’s α subunit. The maximum efficiencies of crosslinking were 10-15% for the most effective reagents, and this value was dependent upon the concentration and length of the crosslinker. In an effort to locate the crosslinking site, monoiodoinsulin was crosslinked to affinity-purified insulin receptor with disuccinimidyl suberate. Limited proteolysis of the hormone/receptor adduct with Staphylococcus aureus V8 protease, chymotrypsin, or thermolysin in an SDS-containing buffer rapidly generated a 55-kDa, insulin-labeled fragment as shown by SDS-PAGE. It was reported earlier that the 55-kDa chymotryptic fragment contained multiple internal SS bonds as evidenced by its shifting mobility on an SDS gel after dithiothreitol treatment. The 55-kDa fragment is also formed by proteolysis of the receptor in the absence of prior insulin crosslinking. This fragment was prepared in amounts sufficient for sequence anal. and was purified by passage successively over gel-permeation and reverse-phase HPLC columns. The sequence of the fragment’s N terminus corresponds to that of the N terminus of the receptor’s α subunit. This fragment also reacts with an antibody raised against a synthetic peptide corresponding to residues 242-253 of the receptor’s α subunit. On the basis of the fragment’s size, N-terminal sequence, and immunoreactivity, the results indicate that the fragment extends from the α subunit’s N terminus through the SS-rich region of this subunit, i.e., residues 155-312. These results are consistent with this region containing the insulin-binding site.
Biochemistry published new progress about 70539-42-3. 70539-42-3 belongs to alcohols-buliding-blocks, auxiliary class pyrrolidine,Ester,Amide,Inhibitor,Inhibitor, name is Bis(2,5-dioxopyrrolidin-1-yl) O,O’-ethane-1,2-diyl disuccinate, and the molecular formula is C19H21N3O3S, Category: alcohols-buliding-blocks.
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