| Autor: |
Lasch, Jürgen, Kudernatsch, Walter, Hanson, Horst |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 1973, Vol. 34 Issue 1, p53-57, 5p |
| Abstrakt: |
An attempt has been made, by means of kinetic experiments, to get some insight into the molecular mechanism of the binding and catalytic steps taking place during low-molecular. weight substrate hydrolysis by leucine aminopeptidase from bovine eye lenses. To this end the variation of the kinetic parameters with concentration and type of well-known activators (anions and metal cations of valency two) was studied systematically. Additional, we searched for substrate-like competitive inhibitors. It was found that the end product L-leucine shows no competition but the compounds N-p-tosyl-N'-butylcarbamide and N-sulfanilyl-N'-butylcarbamide turned out to be rather point competitive inhibitors with Ki values comparable to the Km of L-leucine-p-nitroanilide. The variation of the Ki values with temperature was studied so that the thermodynamic parameters of inhibitor binding could be calculated. In order to be able to make a meaningful comparison between the kinetic parameters all data were subjected to a computer-aided (CDC 1604-A)statistical analysis. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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