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001-es BibID:BIBFORM020961
Első szerző:Austin, Brian P.
Cím:The substrate specificity of Metarhizium anisopliae and Bos taurus carboxypeptidases A : insights into their use as tools for the removal of affinity tags / Austin Brian P., Tözsér József, Bagossi Péter, Tropea Joseph E., Waugh David S.
Dátum:2011
ISSN:1046-5928
Megjegyzések:Carboxypeptidases may serve as tools for removal of C-terminal affinity tags. In the present study, we describe the expression and purification of an A-type carboxypeptidase from the fungal pathogen Metarhizium anisopliae (MeCPA) that has been genetically engineered to facilitate the removal of polyhistidine tags from the C-termini of recombinant proteins. A complete, systematic analysis of the specificity of MeCPA in comparison with that of bovine carboxypeptidase A (BoCPA) was carried out. Our results indicate that the specificity of the two enzymes is similar but not identical. Histidine residues are removed more efficiently by MeCPA. The very inefficient digestion of peptides with C-terminal lysine or arginine residues, along with the complete inability of the enzyme to remove a C-terminal proline, suggests a strategy for designing C-terminal affinity tags that can be trimmed by MeCPA (or BoCPA) to produce a digestion product with a homogeneous endpoint.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Protein Expression And Purification. - 77 : 1 (2011), p. 53-61. -
További szerzők:Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész) Bagossi Péter (1966-2011) (biokémikus, vegyész) Tropea, Joseph E. Waugh, David S.
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001-es BibID:BIBFORM040692
Első szerző:Tőzsér József (molekuláris biológus, biokémikus, vegyész)
Cím:Comparison of the substrate specificity of two potyvirus proteases / Tözsér József, Tropea Joseph E., Cherry Scott, Bagossi Peter, Copeland Terry D., Wlodawer Alexander, Waugh David S.
Dátum:2005
ISSN:1742-464X
Megjegyzések:The substrate specificity of the nuclear inclusion protein a (NIa) proteolytic enzymes from two potyviruses, the tobacco etch virus (TEV) and tobacco vein mottling virus (TVMV), was compared using oligopeptide substrates. Mutations were introduced into TEV protease in an effort to identify key determinants of substrate specificity. The specificity of the mutant enzymes was assessed by using peptides with complementary substitutions. The crystal structure of TEV protease and a homology model of TVMV protease were used to interpret the kinetic data. A comparison of the two structures and the experimental data suggested that the differences in the specificity of the two enzymes may be mainly due to the variation in their S4 and S3 binding subsites. Two key residues predicted to be important for these differences were replaced in TEV protease with the corresponding residues of TVMV protease. Kinetic analyses of the mutants confirmed that these residues play a role in the specificity of the two enzymes. Additional residues in the substrate-binding subsites of TEV protease were also mutated in an effort to alter the specificity of the enzyme.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Febs Journal. - 272 : 2 (2005), p. 514-523. -
További szerzők:Tropea, Joseph E. Cherry, Scott Bagossi Péter (1966-2011) (biokémikus, vegyész) Copeland, Terry D. Wlodawer, Alexander Waugh, David S.
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