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Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas
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| Zeitschriftentitel: | European Journal of Biochemistry |
|---|---|
| Personen und Körperschaften: | , |
| In: | European Journal of Biochemistry, 7, 1968, 1, S. 27-33 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
|
| Schlagwörter: |
| author_facet |
Fiedler, F. Werle, E. Fiedler, F. Werle, E. |
|---|---|
| author |
Fiedler, F. Werle, E. |
| spellingShingle |
Fiedler, F. Werle, E. European Journal of Biochemistry Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas Biochemistry |
| author_sort |
fiedler, f. |
| spelling |
Fiedler, F. Werle, E. 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1968.tb19569.x <jats:p>Kallikrein from porcine pancreas is inhibited by heavy metal ions and activated by sulfhydryl compounds or chelating agents. This activation is interpreted as a reversal of heavy metal inhibition. From the experiments the conclusion is drawn that kallikrein is neither a “sulfhydryl protease” nor a metal‐dependent protease.</jats:p><jats:p>The pH dependency of the hydrolysis of α‐<jats:italic>N</jats:italic>‐benzoyl‐<jats:sc>l</jats:sc>‐arginine ethyl ester by kallikrein at low substrate concentrations indicates three basic groups with <jats:italic>pK</jats:italic> 7.9 and 5.7 in the free enzyme and <jats:italic>pK</jats:italic> 6.9 in the enzyme‐substrate complex which participate in catalysis. This pH‐dependence resembles trypsin‐ and especially cholinesterase‐catalyzed hydrolyses. From the most alkaline <jats:italic>pK</jats:italic> value the participation of an amino group and from the other <jats:italic>pK</jats:italic> values the participation of a histidine residue in kallikrein‐catalyzed hydrolysis is inferred.</jats:p> Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐<i>N</i>‐Benzoyl‐<scp>l</scp>‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas European Journal of Biochemistry |
| doi_str_mv |
10.1111/j.1432-1033.1968.tb19569.x |
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Online Free |
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Chemie und Pharmazie |
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Wiley, 1968 |
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Wiley, 1968 |
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0014-2956 1432-1033 |
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0014-2956 1432-1033 |
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1968 |
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European Journal of Biochemistry |
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49 |
| title |
Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_unstemmed |
Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_full |
Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_fullStr |
Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_full_unstemmed |
Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_short |
Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_sort |
activation, inhibition, and ph‐dependence of the hydrolysis of α‐<i>n</i>‐benzoyl‐<scp>l</scp>‐arginine ethyl ester catalyzed by kallikrein from porcine pancreas |
| topic |
Biochemistry |
| url |
http://dx.doi.org/10.1111/j.1432-1033.1968.tb19569.x |
| publishDate |
1968 |
| physical |
27-33 |
| description |
<jats:p>Kallikrein from porcine pancreas is inhibited by heavy metal ions and activated by sulfhydryl compounds or chelating agents. This activation is interpreted as a reversal of heavy metal inhibition. From the experiments the conclusion is drawn that kallikrein is neither a “sulfhydryl protease” nor a metal‐dependent protease.</jats:p><jats:p>The pH dependency of the hydrolysis of α‐<jats:italic>N</jats:italic>‐benzoyl‐<jats:sc>l</jats:sc>‐arginine ethyl ester by kallikrein at low substrate concentrations indicates three basic groups with <jats:italic>pK</jats:italic> 7.9 and 5.7 in the free enzyme and <jats:italic>pK</jats:italic> 6.9 in the enzyme‐substrate complex which participate in catalysis. This pH‐dependence resembles trypsin‐ and especially cholinesterase‐catalyzed hydrolyses. From the most alkaline <jats:italic>pK</jats:italic> value the participation of an amino group and from the other <jats:italic>pK</jats:italic> values the participation of a histidine residue in kallikrein‐catalyzed hydrolysis is inferred.</jats:p> |
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| description | <jats:p>Kallikrein from porcine pancreas is inhibited by heavy metal ions and activated by sulfhydryl compounds or chelating agents. This activation is interpreted as a reversal of heavy metal inhibition. From the experiments the conclusion is drawn that kallikrein is neither a “sulfhydryl protease” nor a metal‐dependent protease.</jats:p><jats:p>The pH dependency of the hydrolysis of α‐<jats:italic>N</jats:italic>‐benzoyl‐<jats:sc>l</jats:sc>‐arginine ethyl ester by kallikrein at low substrate concentrations indicates three basic groups with <jats:italic>pK</jats:italic> 7.9 and 5.7 in the free enzyme and <jats:italic>pK</jats:italic> 6.9 in the enzyme‐substrate complex which participate in catalysis. This pH‐dependence resembles trypsin‐ and especially cholinesterase‐catalyzed hydrolyses. From the most alkaline <jats:italic>pK</jats:italic> value the participation of an amino group and from the other <jats:italic>pK</jats:italic> values the participation of a histidine residue in kallikrein‐catalyzed hydrolysis is inferred.</jats:p> |
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| imprint | Wiley, 1968 |
| imprint_str_mv | Wiley, 1968 |
| institution | DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-D161, DE-Zwi2, DE-Gla1, DE-Zi4, DE-15 |
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| mega_collection | Wiley (CrossRef) |
| physical | 27-33 |
| publishDate | 1968 |
| publishDateSort | 1968 |
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| recordtype | ai |
| series | European Journal of Biochemistry |
| source_id | 49 |
| spelling | Fiedler, F. Werle, E. 0014-2956 1432-1033 Wiley Biochemistry http://dx.doi.org/10.1111/j.1432-1033.1968.tb19569.x <jats:p>Kallikrein from porcine pancreas is inhibited by heavy metal ions and activated by sulfhydryl compounds or chelating agents. This activation is interpreted as a reversal of heavy metal inhibition. From the experiments the conclusion is drawn that kallikrein is neither a “sulfhydryl protease” nor a metal‐dependent protease.</jats:p><jats:p>The pH dependency of the hydrolysis of α‐<jats:italic>N</jats:italic>‐benzoyl‐<jats:sc>l</jats:sc>‐arginine ethyl ester by kallikrein at low substrate concentrations indicates three basic groups with <jats:italic>pK</jats:italic> 7.9 and 5.7 in the free enzyme and <jats:italic>pK</jats:italic> 6.9 in the enzyme‐substrate complex which participate in catalysis. This pH‐dependence resembles trypsin‐ and especially cholinesterase‐catalyzed hydrolyses. From the most alkaline <jats:italic>pK</jats:italic> value the participation of an amino group and from the other <jats:italic>pK</jats:italic> values the participation of a histidine residue in kallikrein‐catalyzed hydrolysis is inferred.</jats:p> Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐<i>N</i>‐Benzoyl‐<scp>l</scp>‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas European Journal of Biochemistry |
| spellingShingle | Fiedler, F., Werle, E., European Journal of Biochemistry, Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas, Biochemistry |
| title | Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_full | Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_fullStr | Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_full_unstemmed | Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_short | Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| title_sort | activation, inhibition, and ph‐dependence of the hydrolysis of α‐<i>n</i>‐benzoyl‐<scp>l</scp>‐arginine ethyl ester catalyzed by kallikrein from porcine pancreas |
| title_unstemmed | Activation, Inhibition, and pH‐Dependence of the Hydrolysis of α‐N‐Benzoyl‐l‐Arginine Ethyl Ester Catalyzed by Kallikrein from Porcine Pancreas |
| topic | Biochemistry |
| url | http://dx.doi.org/10.1111/j.1432-1033.1968.tb19569.x |