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...

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Autores principales: Santa-Coloma, T.A., Muschietti, J.P., Charreau, E.H.
Formato: JOUR
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: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 todo:paper_03009629_v85_n3_p401_SantaColoma
record_format dspace
spelling todo:paper_03009629_v85_n3_p401_SantaColoma2023-10-03T15:18:10Z Sex steroid binding protein from Bufo arenarum: Further characterization Santa-Coloma, T.A. Muschietti, J.P. Charreau, E.H. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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
Santa-Coloma, T.A.
Muschietti, J.P.
Charreau, E.H.
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.
format JOUR
author Santa-Coloma, T.A.
Muschietti, J.P.
Charreau, E.H.
author_facet Santa-Coloma, T.A.
Muschietti, J.P.
Charreau, E.H.
author_sort Santa-Coloma, T.A.
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
url http://hdl.handle.net/20.500.12110/paper_03009629_v85_n3_p401_SantaColoma
work_keys_str_mv AT santacolomata sexsteroidbindingproteinfrombufoarenarumfurthercharacterization
AT muschiettijp sexsteroidbindingproteinfrombufoarenarumfurthercharacterization
AT charreaueh sexsteroidbindingproteinfrombufoarenarumfurthercharacterization
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