Sex steroid binding protein from Bufo arenarum: Further characterization

1. 1. The effects of temperature, pH, divalent cations, 2-mercaptoethanol (Et-SH), N-ethylmaleimide (NEM), and phenylmethylsulfonyl fluoride (PMSF) on the dihydrotestosterone (DHT) binding to sex steroid binding protein from Bufo arenarum (baSBP) were examined. 2. 2. The temperature curve indicated...

Descripción completa

Guardado en:
Detalles Bibliográficos
Publicado: 1986
Materias:
benzylsulfonyl fluoride
mercaptoethanol
n ethylmaleimide
radioisotope
androstanolone h 3
animal cell
drug protein binding
nonhuman
priority journal
Animal
Bufo arenarum
Female
Hydrogen-Ion Concentration
Kinetics
Sex Hormone-Binding Globulin
Stanolone
Thermodynamics
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03009629_v85_n3_p401_SantaColoma
http://hdl.handle.net/20.500.12110/paper_03009629_v85_n3_p401_SantaColoma
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_03009629_v85_n3_p401_SantaColoma
record_format dspace
spelling paper:paper_03009629_v85_n3_p401_SantaColoma2023-06-08T15:27:46Z Sex steroid binding protein from Bufo arenarum: Further characterization benzylsulfonyl fluoride mercaptoethanol n ethylmaleimide radioisotope androstanolone h 3 animal cell drug protein binding nonhuman priority journal Animal Bufo arenarum Female Hydrogen-Ion Concentration Kinetics Sex Hormone-Binding Globulin Stanolone Thermodynamics 1. 1. The effects of temperature, pH, divalent cations, 2-mercaptoethanol (Et-SH), N-ethylmaleimide (NEM), and phenylmethylsulfonyl fluoride (PMSF) on the dihydrotestosterone (DHT) binding to sex steroid binding protein from Bufo arenarum (baSBP) were examined. 2. 2. The temperature curve indicated that the binding remained stable up to 50°C and the pH curve showed maximum binding between pH 7 and 9. 3. 3. The incubations of baSBP with divalent cations, NEM and Et-SH demonstrated that baSBP require disulfides and sulfhydryl groups for steroid binding or to maintain an adequate protein conformation. 4. 4. On the other hand, PMSF had no effect on the binding, consequently, serine residues appear not to be involved in DHT binding to baSBP. 5. 5. These results indicate that baSBP has a behavior resembling that of human SBP. © 1986. 1986 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03009629_v85_n3_p401_SantaColoma http://hdl.handle.net/20.500.12110/paper_03009629_v85_n3_p401_SantaColoma
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic benzylsulfonyl fluoride
mercaptoethanol
n ethylmaleimide
radioisotope
androstanolone h 3
animal cell
drug protein binding
nonhuman
priority journal
Animal
Bufo arenarum
Female
Hydrogen-Ion Concentration
Kinetics
Sex Hormone-Binding Globulin
Stanolone
Thermodynamics
spellingShingle benzylsulfonyl fluoride
mercaptoethanol
n ethylmaleimide
radioisotope
androstanolone h 3
animal cell
drug protein binding
nonhuman
priority journal
Animal
Bufo arenarum
Female
Hydrogen-Ion Concentration
Kinetics
Sex Hormone-Binding Globulin
Stanolone
Thermodynamics
Sex steroid binding protein from Bufo arenarum: Further characterization
topic_facet benzylsulfonyl fluoride
mercaptoethanol
n ethylmaleimide
radioisotope
androstanolone h 3
animal cell
drug protein binding
nonhuman
priority journal
Animal
Bufo arenarum
Female
Hydrogen-Ion Concentration
Kinetics
Sex Hormone-Binding Globulin
Stanolone
Thermodynamics
description 1. 1. The effects of temperature, pH, divalent cations, 2-mercaptoethanol (Et-SH), N-ethylmaleimide (NEM), and phenylmethylsulfonyl fluoride (PMSF) on the dihydrotestosterone (DHT) binding to sex steroid binding protein from Bufo arenarum (baSBP) were examined. 2. 2. The temperature curve indicated that the binding remained stable up to 50°C and the pH curve showed maximum binding between pH 7 and 9. 3. 3. The incubations of baSBP with divalent cations, NEM and Et-SH demonstrated that baSBP require disulfides and sulfhydryl groups for steroid binding or to maintain an adequate protein conformation. 4. 4. On the other hand, PMSF had no effect on the binding, consequently, serine residues appear not to be involved in DHT binding to baSBP. 5. 5. These results indicate that baSBP has a behavior resembling that of human SBP. © 1986.
title Sex steroid binding protein from Bufo arenarum: Further characterization
title_short Sex steroid binding protein from Bufo arenarum: Further characterization
title_full Sex steroid binding protein from Bufo arenarum: Further characterization
title_fullStr Sex steroid binding protein from Bufo arenarum: Further characterization
title_full_unstemmed Sex steroid binding protein from Bufo arenarum: Further characterization
title_sort sex steroid binding protein from bufo arenarum: further characterization
publishDate 1986
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03009629_v85_n3_p401_SantaColoma
http://hdl.handle.net/20.500.12110/paper_03009629_v85_n3_p401_SantaColoma
_version_ 1768545646578499584

Ejemplares similares