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Size and Stereospecificity of the Active Site of Porcine Elastase
Daphne Atlas
*
, Arieh Berger
*
Corresponding author for this work
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peer-review
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Scopus citations
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Keyphrases
Active Sites
100%
Porcine
100%
Elastase
100%
Stereospecificity
100%
Kcat
50%
P-nitrophenyl Esters
50%
TETRA
25%
Binding Mode
25%
D-form
25%
Enzymatic Hydrolysis
25%
Peptide Substrate
25%
Ester Hydrolysis
25%
Catalytic Power
25%
Ester Bond
25%
Biochemistry, Genetics and Molecular Biology
Active Site
100%
Stereospecificity
100%
Elastase
100%
Enzymatic Hydrolysis
50%
Turnover Number
50%
N-Terminus
25%