The interaction of papain with polycations
| Autor: | J B Lawton, R J Washington, C I Mekras |
|---|---|
| Rok vydání: | 1989 |
| Předmět: |
Protein Denaturation
Chemical Phenomena Size-exclusion chromatography Pharmaceutical Science Spermine Catalysis chemistry.chemical_compound Hemoglobins Cations Papain Humans Polylysine Protamines Pharmacology chemistry.chemical_classification Dansyl Compounds Chromatography Cyanides biology Substrate (chemistry) Povidone Protamine Spermidine Chemistry Enzyme Spectrometry Fluorescence chemistry Biophysics biology.protein Chromatography Gel Fluorescence anisotropy |
| Zdroj: | The Journal of pharmacy and pharmacology. 41(1) |
| ISSN: | 0022-3573 |
| Popis: | An investigation has been made of the interactions of the enzyme papain with the polycations protamine, polybrene, poly(L-lysine), spermine, spermidine and the neutral polymer polyvinylpyrrolidone (PVP). At low concentrations, each behaves as an inhibitor of the enzyme. As their concentrations increased above a certain level, the activity of the systems increased, and their inhibition of the enzyme appeared to be less pronounced. When acting by themselves in the presence of the substrate haemoglobin, each of the polycations was a weak proteolytic catalyst with a ranking of catalytic effectiveness of protamine > polybrene > poly(L-lysine) > polyvinyl-pyrrolidone > spermidine > spermine. This effect could explain the anomalous inhibition of papain by these polycations. The interaction of papain with dansyl protamine (DNSP) and the extent of complex formation were studied using a fluorescence polarization technique and the results showed that there was a strong interaction occurred. The strength of binding was assessed by determination of the critical electrolyte concentration (0·2 M, NaNO3). The stoichiometry of the DNSP-papain complex was found to be 63 base moles of DNSP to one mole of papain. |
| Databáze: | OpenAIRE |
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