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G Kaslik

Showing results (1-10 of 6) with videos related to

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FEBS Letters|August 21, 1995
Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibilityG Kaslik, A Patthy, M Bálint, et al.
European Journal of Biochemistry|January 23, 1999
The differential specificity of chymotrypsin A and B is determined by amino acid 226P Hudáky, G Kaslik, I Venekei, et al.
European Journal of Biochemistry|December 6, 2001
Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsinA Bódi, G Kaslik, I Venekei, et al.
Archives of Biochemistry and Biophysics|February 17, 1999
Properties of the His57-Asp102 dyad of rat trypsin D189S in the zymogen, activated enzyme, and alpha1-proteinase inhibitor complexed formsG Kaslik, W M Westler, L Gráf, et al.
The Journal of Biological Chemistry|April 20, 2001
Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitisL Szilágyi, E Kénesi, G Katona, et al.
Biochemistry|May 6, 1997
Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active siteG Kaslik, J Kardos, E Szabó, et al.
Pageof 1

Showing results (1-10 of 6) with videos related to

Sort By:
Pageof 1
FEBS Letters|August 21, 1995
Trypsin complexed with alpha 1-proteinase inhibitor has an increased structural flexibilityG Kaslik, A Patthy, M Bálint, et al.
European Journal of Biochemistry|January 23, 1999
The differential specificity of chymotrypsin A and B is determined by amino acid 226P Hudáky, G Kaslik, I Venekei, et al.
European Journal of Biochemistry|December 6, 2001
Structural determinants of the half-life and cleavage site preference in the autolytic inactivation of chymotrypsinA Bódi, G Kaslik, I Venekei, et al.
Archives of Biochemistry and Biophysics|February 17, 1999
Properties of the His57-Asp102 dyad of rat trypsin D189S in the zymogen, activated enzyme, and alpha1-proteinase inhibitor complexed formsG Kaslik, W M Westler, L Gráf, et al.
The Journal of Biological Chemistry|April 20, 2001
Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitisL Szilágyi, E Kénesi, G Katona, et al.
Biochemistry|May 6, 1997
Effects of serpin binding on the target proteinase: global stabilization, localized increased structural flexibility, and conserved hydrogen bonding at the active siteG Kaslik, J Kardos, E Szabó, et al.
Pageof 1