Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein
(1984) In Scandinavian Journal of Clinical and Laboratory Investigation 44(5). p.439-446- Abstract
From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose® chromatography was followed by gel filtration (Biogel® P 60) and by fast performance liquid chromatography on a reversed phase column (C8). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a PI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the... (More)
From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose® chromatography was followed by gel filtration (Biogel® P 60) and by fast performance liquid chromatography on a reversed phase column (C8). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a PI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the protein sequence is unique: HNKQEGRDHDKSKG HFHRVVIHHKGGKAHRG-.A specific rabbit antiserum was raised against the 12.8 kDa basic protein. The protein was found to be unique to seminal plasma among all extracellular fluids examined. Three immunologically related 52 kDa, 71 kDa, and 76 kDa proteins were identified in seminal vesicle secretion when it had been reduced. Prostatic enzyme(s) degraded these proteins to the 12.8 kDa basic protein and several other basic proteins with apparent molecular masses below 18 kDa.
(Less)
- author
- Lilja, H. LU ; Laurell, C. B. LU and Jeppsson, J. O. LU
- organization
- publishing date
- 1984
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Peptide fragments, Prostate, Protease inhibitors, Semen, Seminal vesicles
- in
- Scandinavian Journal of Clinical and Laboratory Investigation
- volume
- 44
- issue
- 5
- pages
- 439 - 446
- publisher
- Informa Healthcare
- external identifiers
-
- pmid:6484484
- scopus:0021233719
- ISSN
- 0036-5513
- DOI
- 10.3109/00365518409083835
- language
- English
- LU publication?
- yes
- id
- b12b7852-9d44-456f-a434-f512b39ecd53
- date added to LUP
- 2022-12-06 16:58:54
- date last changed
- 2024-01-03 19:32:27
@article{b12b7852-9d44-456f-a434-f512b39ecd53, abstract = {{<p>From liquefied human seminal plasma, we purified the predominant basic protein which appears following liquefaction of coagulated semen. The protein was purified in the presence of di-isopropylfluorophosphate to retard its degradation. Heparin-Sepharose® chromatography was followed by gel filtration (Biogel® P 60) and by fast performance liquid chromatography on a reversed phase column (C<sub>8</sub>). The basic protein is a single polypeptide chain with an apparent molecular mass of 12.8 kDa, and has a PI value between that of trypsinogen (9.3) and cytochrome C (10.3). The protein contains no carbohydrate, is rich in histidine, glutamate, and lysine, but is devoid of both cysteine and methionine. The amino-terminal portion of the protein sequence is unique: HNKQEGRDHDKSKG HFHRVVIHHKGGKAHRG-.A specific rabbit antiserum was raised against the 12.8 kDa basic protein. The protein was found to be unique to seminal plasma among all extracellular fluids examined. Three immunologically related 52 kDa, 71 kDa, and 76 kDa proteins were identified in seminal vesicle secretion when it had been reduced. Prostatic enzyme(s) degraded these proteins to the 12.8 kDa basic protein and several other basic proteins with apparent molecular masses below 18 kDa.</p>}}, author = {{Lilja, H. and Laurell, C. B. and Jeppsson, J. O.}}, issn = {{0036-5513}}, keywords = {{Peptide fragments; Prostate; Protease inhibitors; Semen; Seminal vesicles}}, language = {{eng}}, number = {{5}}, pages = {{439--446}}, publisher = {{Informa Healthcare}}, series = {{Scandinavian Journal of Clinical and Laboratory Investigation}}, title = {{Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein}}, url = {{http://dx.doi.org/10.3109/00365518409083835}}, doi = {{10.3109/00365518409083835}}, volume = {{44}}, year = {{1984}}, }