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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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
Descripción
Sumario: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.

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