Open AccessThe self‐association of protein SV‐IV and its possible functional implications
Author(s) -
Stiuso Paola,
Metafora Salvatore,
Facchiano Angelo M.,
Colonna Giovanni,
Ragone Raffaele
Publication year - 1999
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1327.1999.00944.x
Subject(s) - chemistry , protein secondary structure , fluorescence , absorption (acoustics) , biophysics , protein structure , biochemistry , biology , materials science , physics , quantum mechanics , composite material
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.