Structural heterogeneity, post-translational modifications, and biological activities of SV-IV, a major protein secreted from the rat seminal vesicle epithelium.
Rapid Commun Mass Spectrom
; 11(9): 1007-14, 1997.
Article
in En
| MEDLINE
| ID: mdl-9204575
ABSTRACT
The primary structure of purified SV-IV, a major secretory protein synthesized by the rat seminal vesicle (SV) epithelium, was analysed by electrospray mass spectrometry (ES-MS). The protein was found to be highly heterogeneous. The various components were separated and identified by reversed phase high-performance liquid chromatography (HPLC) on line with ES-MS. Structural characterization of the SV-IV cyanogen bromide digests revealed the occurrence of a Val/Met substitution in about 50% of the purified protein molecules. We suggest that this mutation is the expression of a genetic polymorphism. Other minor components, corresponding to structural changes (fragmentation, deletion, and phosphorylation) of SV-IV and probably due to post-translational modifications of the native protein, were also detected. In particular, by using protein tyrosine phosphatase hydrolysis combined with ES-MS, we demonstrated that, in the phosphorylated species of SV-IV, a single phosphate group was covalently bound to the Tyr-36 residue. The significance of these findings in relation to the regulation of important biological processes, such as immune response, blood coagulation, inflammatory reaction, and mammalian reproduction, are discussed.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Seminal Vesicles
/
Proteins
/
Prostatic Secretory Proteins
Type of study:
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
Rapid Commun Mass Spectrom
Year:
1997
Document type:
Article