Primary Structure of Triosephosphate Isomerase from Bacillus stearothermophilus

Publisher Website
Google Scholar
Abstract
Triosephosphate isomerase from B. stearothermophilus is a dimeric enzyme comprising 2 chemically identical polypeptide chains. The nearly complete amino acid sequence of the subunit polypeptide chain was established from sequences of tryptic, chymotryptic and lysine-blocked tryptic fragments of S-[2-14C]carboxymethylated enzyme. Overlaps not established by experimental data were provisionally established from considerations of sequence homology with previously established sequences for the rabbit, chicken and coelacanth enzymes. The nearly complete sequence of the 249 residues is given.