L-usnate-urease interactions: binding sites for the ligand.
نویسندگان
چکیده
L-usnic acid inactivates urease by formation of high molecular weight aggregates which can reached by a maximum of 880 000. L-cysteine partially reverses the inactivation of stimulating the appearance of active high molecular weight polymers. The existence of two class of binding points for L-usnic acid on the urease molecule is proposed, the first showing high affinity for the ligand, related with the loss of activity, and the second, of low affinity, related to polymerization process.
منابع مشابه
L-usnate-urease interactions: binding sites for polymerization.
L-usnic acid inactivates urease through a process which implicates the blockade of--SH groups in parallel to the formation of inactive polymers. Both L-alanine and L-proline partially reverses the inactivation and effectively diminishes the amount of highly polymerized protein. The amino acids also prevent the linkage of L-usnic acid on the sites of low affinity for the ligand, being then relat...
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عنوان ژورنال:
- Zeitschrift fur Naturforschung. Section C, Biosciences
دوره 35 11-12 شماره
صفحات -
تاریخ انتشار 1980