Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:6.3.4.6 (urease)
 7,490 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Protein aggregation is believed to be due to conformers that expose hydrophobic clusters that promote protein association. Such conformers can be detected using a fluorescent probe like 8-anilino 1-naphthalenesulfonic acid (ANSA). Here we show that urease exposed to 1.0 M guanidine-hydrogen chloride has a higher affinity for ANSA that native or denatured urease. The binding occurs over a narrow range of denaturant concentration, well below the concentration required to induce denaturation. The impact of ANSA on urease aggregation was further studied by fluorescence, light-scattering, and activity measurements. We found that ANSA modifies urease aggregates and can provide partial protection against inactivation arising from thermally induced aggregation. It seems that the well-known susceptibility of urease to aggregation is due to an intermediate that can be populated in the absence of denaturation. Such a rationale would explain why folding stability of urease is a poor indicator of long-term stabilization by various media.
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PMID:Detection of an unfolding intermediate in alpha-urease with enhanced affinity for ANSA. 919 74