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K Breddam

Showing results (31-40 of 52) with videos related to

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FEBS Letters|December 9, 1991
Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acidS B Sørensen, T L Sørensen, K Breddam
Journal of Molecular Biology|February 9, 1996
Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificityT L Bullock, K Breddam, S J Remington
Applied and Environmental Microbiology|July 1, 1992
Purification and characterization of two serine carboxypeptidases from Aspergillus niger and their use in C-terminal sequencing of proteins and peptide synthesisF Dal Degan, B Ribadeau-Dumas, K Breddam
Biochemistry|November 2, 1993
A glutamic acid specific serine protease utilizes a novel histidine triad in substrate bindingV L Nienaber, K Breddam, J J Birktoft
FEBS Letters|February 3, 1992
Introduction of a free cysteinyl residue at position 68 in the subtilisin Savinase, based on homology with proteinase KL M Bech, S Branner, S Hastrup, et al.
Journal of Bacteriology|April 1, 1992
Proline-specific endopeptidases from microbial sources: isolation of an enzyme from a Xanthomonas spE Szwajcer-Dey, J Rasmussen, M Meldal, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 12, 1994
Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificityM Meldal, I Svendsen, K Breddam, et al.
European Journal of Biochemistry|December 27, 1990
A highly active and oxidation-resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modificationH Grøn, L M Bech, S Branner, et al.
Biochemistry|April 17, 1979
Carboxypeptidase of Streptomyces griseus. Implications of its characteristicsK Breddam, T J Bazzone, B Holmquist, et al.
Biochemistry|September 7, 1993
Mutational replacements of the amino acid residues forming the hydrophobic S4 binding pocket of subtilisin 309 from Bacillus lentusS B Sørensen, L M Bech, M Meldal, et al.
Pageof 6

Showing results (31-40 of 52) with videos related to

Sort By:
Pageof 6
FEBS Letters|December 9, 1991
Fragmentation of proteins by S. aureus strain V8 protease. Ammonium bicarbonate strongly inhibits the enzyme but does not improve the selectivity for glutamic acidS B Sørensen, T L Sørensen, K Breddam
Journal of Molecular Biology|February 9, 1996
Peptide aldehyde complexes with wheat serine carboxypeptidase II: implications for the catalytic mechanism and substrate specificityT L Bullock, K Breddam, S J Remington
Applied and Environmental Microbiology|July 1, 1992
Purification and characterization of two serine carboxypeptidases from Aspergillus niger and their use in C-terminal sequencing of proteins and peptide synthesisF Dal Degan, B Ribadeau-Dumas, K Breddam
Biochemistry|November 2, 1993
A glutamic acid specific serine protease utilizes a novel histidine triad in substrate bindingV L Nienaber, K Breddam, J J Birktoft
FEBS Letters|February 3, 1992
Introduction of a free cysteinyl residue at position 68 in the subtilisin Savinase, based on homology with proteinase KL M Bech, S Branner, S Hastrup, et al.
Journal of Bacteriology|April 1, 1992
Proline-specific endopeptidases from microbial sources: isolation of an enzyme from a Xanthomonas spE Szwajcer-Dey, J Rasmussen, M Meldal, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 12, 1994
Portion-mixing peptide libraries of quenched fluorogenic substrates for complete subsite mapping of endoprotease specificityM Meldal, I Svendsen, K Breddam, et al.
European Journal of Biochemistry|December 27, 1990
A highly active and oxidation-resistant subtilisin-like enzyme produced by a combination of site-directed mutagenesis and chemical modificationH Grøn, L M Bech, S Branner, et al.
Biochemistry|April 17, 1979
Carboxypeptidase of Streptomyces griseus. Implications of its characteristicsK Breddam, T J Bazzone, B Holmquist, et al.
Biochemistry|September 7, 1993
Mutational replacements of the amino acid residues forming the hydrophobic S4 binding pocket of subtilisin 309 from Bacillus lentusS B Sørensen, L M Bech, M Meldal, et al.
Pageof 6