The self-association of protein SV-IV and its possible functional implications.
Eur J Biochem
; 266(3): 1029-35, 1999 Dec.
Article
en En
| MEDLINE
| ID: mdl-10583398
ABSTRACT
The protein SV-IV, a major protein secreted from the rat seminal vesicle epithelium, is a basic protein with immunomodulatory, anti-inflammatory, and procoagulant activity. Predictions suggested that this protein is very flexible, with its three tyrosyl residues presumably located in water-exposed segments of the primary structure. The solution behaviour of the protein was investigated by two types of spectroscopic techniques. Modifications of the spectral characteristics of tyrosyl residues induced by changes of protein concentration were demonstrated by absorption and fluorescence experiments. In addition, secondary structure rearrangements associated with a possible self-association equilibrium were highlighted by far-UV CD spectra. The equilibrium, confirmed by chromatographic techniques, appears to control some biological properties of the protein.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Vesículas Seminales
/
Proteínas
Tipo de estudio:
Prognostic_studies
/
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
Eur J Biochem
Año:
1999
Tipo del documento:
Article
País de afiliación:
Italia