PMID: 9535275Apr 16, 1998Paper

Studies of the M15 beta-galactosidase complementation process

Journal of Protein Chemistry
C N Gallagher, R E Huber

Abstract

M15 beta-Galactosidase was activated by heat-denatured wild-type beta-galactosidase, urea, and heat-denatured wild-type beta-galactosidase, a peptide made up of residues 6-44 of beta-galactosidase and CB2, the peptide that is normally used for complementation (residues 3-92 of beta-galactosidase). In each case roughly equal activation levels were attained. Heat-denatured wild-type beta-galactosidase was present as a finely divided visible white precipitate both before and after complementation. The heat-denatured protein by itself did not migrate on native PAGE and both the protein and the activity that occurred as a result of the complementation also remained at the point of application. The N-terminal ends of the heat-denatured wild-type beta-galactosidase must have been available for complementation and must have been mobile enough to allow tetramer to form despite being aggregated. Beta-galactosidase denatured by both urea and heat resulted in a streak of interacting protein on the native PAGE. Upon activation, a streak (indicating that interaction was still occurring) was still present, but it moves more slowly. Complementation using a peptide called XP (made up of residues 6-44 plus an additional nine C-terminal amino aci...Continue Reading

Citations

Mar 6, 2015·Protein Science : a Publication of the Protein Society·Kotaro NishiyamaTetsuya Yomo
Sep 27, 2012·Protein Science : a Publication of the Protein Society·Douglas H JuersReuben E Huber

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