Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour

1. 1. Kinetic studies were carried out on the soluble and immobilized Rhodanese. 2. 2. The soluble enzyme showed a typical Michaelis-Menten behaviour, an inhibitory effect was observed at high thiosulphate and cyanide concentrations. 3. 3. The product sulphite was also an inhibitor, instead thiocyan...

Descripción completa

Detalles Bibliográficos
Publicado: 1987
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n12_p1199_Vazquez
http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n12_p1199_Vazquez
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_0020711X_v19_n12_p1199_Vazquez
record_format dspace
spelling paper:paper_0020711X_v19_n12_p1199_Vazquez2023-06-08T14:41:08Z Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour 1. 1. Kinetic studies were carried out on the soluble and immobilized Rhodanese. 2. 2. The soluble enzyme showed a typical Michaelis-Menten behaviour, an inhibitory effect was observed at high thiosulphate and cyanide concentrations. 3. 3. The product sulphite was also an inhibitor, instead thiocyanate increased the enzyme velocity when it was added to the incubation mixture. 4. 4. A ping-pong mechanism was proposed for Rp. palustris Rhodanese with a stable (free enzyme: E) and an unstable (sulfur substituted enzyme: ES) kinetic enzyme form. 5. 5. The insolubilized Rhodanese presented an unusual kinetic behaviour, with sigmoid shape substrate profiles and non-linear double reciprocal plots. 6. 6. From the empirical Hill equation, positive cooperativity (n>1) was found for both substrates. © 1987. 1987 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n12_p1199_Vazquez http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n12_p1199_Vazquez
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
description 1. 1. Kinetic studies were carried out on the soluble and immobilized Rhodanese. 2. 2. The soluble enzyme showed a typical Michaelis-Menten behaviour, an inhibitory effect was observed at high thiosulphate and cyanide concentrations. 3. 3. The product sulphite was also an inhibitor, instead thiocyanate increased the enzyme velocity when it was added to the incubation mixture. 4. 4. A ping-pong mechanism was proposed for Rp. palustris Rhodanese with a stable (free enzyme: E) and an unstable (sulfur substituted enzyme: ES) kinetic enzyme form. 5. 5. The insolubilized Rhodanese presented an unusual kinetic behaviour, with sigmoid shape substrate profiles and non-linear double reciprocal plots. 6. 6. From the empirical Hill equation, positive cooperativity (n>1) was found for both substrates. © 1987.
title Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour
spellingShingle Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour
title_short Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour
title_full Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour
title_fullStr Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour
title_full_unstemmed Soluble and immobilized RP. palustris rhodanese-II. Some particular kinetic behaviour
title_sort soluble and immobilized rp. palustris rhodanese-ii. some particular kinetic behaviour
publishDate 1987
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v19_n12_p1199_Vazquez
http://hdl.handle.net/20.500.12110/paper_0020711X_v19_n12_p1199_Vazquez
_version_ 1768544211254116352

Ejemplares similares