Inhibition of lysozyme by polyvalent metal ions

Fred Ostroy, Richard A. Gams, Jerry D. Glickson, Robert E. Lenkinski

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Abstract

The rate of hen egg-white lysozyme (mucopeptide N-acetylmuramoylhydrolase, EC 3.2.1.17), catalysis was determined in the presence of various metal ions (CO2+, Zn2+ and eight of the trivalent lanthanide ions). In the assay system employed, the lanthanides were found to inhibit more strongly than either Zn2+ or Co2+. The inhibition data was fitted to several models of the interactions of the metal ion with the enzyme. These models ranged in complexity from a single inhibitory metal binding site on the enzyme (two-parameter fit) to the presence of two non-independent and non-equivalent inhibitory metal binding sites (five-parameter fit). The more complicated models did not fit the data more precisely than the simplest one-site model, suggesting that the adoption of the simpler model is warranted. The fact that association constants obtained from the simplest analysis for Co2+ (1.3 ± 1.9 · 102 M-1) and Gd3+ (7.0 ± 2.6 · 103 M-1) are consistent with literature values determined from spectroscopic measurements further supports the validity of the simplest model.

Original languageEnglish (US)
Pages (from-to)56-62
Number of pages7
JournalBBA - Enzymology
Volume527
Issue number1
DOIs
Publication statusPublished - Nov 10 1978

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ASJC Scopus subject areas

  • Medicine(all)

Cite this

Ostroy, F., Gams, R. A., Glickson, J. D., & Lenkinski, R. E. (1978). Inhibition of lysozyme by polyvalent metal ions. BBA - Enzymology, 527(1), 56-62. https://doi.org/10.1016/0005-2744(78)90255-3