beta-Microseminoprotein binds CRISP-3 in human seminal plasma
(2005) In Biochemical and Biophysical Research Communications 333(2). p.555-561- Abstract
- P-Microseminoprotein (MSP) and cysteine-rich secretory protein 3 (CRISP-3) are abundant constituents of human seminal plasma. Immunoprecipitation and gel filtration of seminal plasma proteins combined with examination of the proteins in their pure form showed that MSP and CRISP-3 form stable, non-covalent complexes. CRISP-3 binds MSP with very high affinity, as evidenced by surface plasmon resonance. Due to far higher abundance of MSP in prostatic fluid, it manifests large overcapacity for CRISP-3 binding. Structural similarity with an MSP-binding protein from blood plasma suggests that CRISP-3 binds MSP through its ami-terminal SCP-domain.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/233179
- author
- Udby, L ; Lundwall, Åke LU ; Johnsen, A H ; Fernlund, Per LU ; Valtonen-André, Camilla LU ; Blom, Anna LU ; Lilja, Hans LU ; Borregaard, N ; Kieldsen, L and Bjartell, Anders LU
- organization
- publishing date
- 2005
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- mass, spectrometry, surface plasmon resonance, SCP-domain, protein complex, prostate cancer, seminal plasma, PSP94, cysteine-rich secretory protein, beta-microseminoprotein
- in
- Biochemical and Biophysical Research Communications
- volume
- 333
- issue
- 2
- pages
- 555 - 561
- publisher
- Elsevier
- external identifiers
-
- wos:000230418700039
- pmid:15950934
- scopus:20544459894
- ISSN
- 1090-2104
- DOI
- 10.1016/j.bbrc.2005.05.139
- language
- English
- LU publication?
- yes
- id
- eb056506-9840-4bce-9b89-ed0a9b3a2c0b (old id 233179)
- date added to LUP
- 2016-04-01 16:49:49
- date last changed
- 2022-03-15 03:16:56
@article{eb056506-9840-4bce-9b89-ed0a9b3a2c0b, abstract = {{P-Microseminoprotein (MSP) and cysteine-rich secretory protein 3 (CRISP-3) are abundant constituents of human seminal plasma. Immunoprecipitation and gel filtration of seminal plasma proteins combined with examination of the proteins in their pure form showed that MSP and CRISP-3 form stable, non-covalent complexes. CRISP-3 binds MSP with very high affinity, as evidenced by surface plasmon resonance. Due to far higher abundance of MSP in prostatic fluid, it manifests large overcapacity for CRISP-3 binding. Structural similarity with an MSP-binding protein from blood plasma suggests that CRISP-3 binds MSP through its ami-terminal SCP-domain.}}, author = {{Udby, L and Lundwall, Åke and Johnsen, A H and Fernlund, Per and Valtonen-André, Camilla and Blom, Anna and Lilja, Hans and Borregaard, N and Kieldsen, L and Bjartell, Anders}}, issn = {{1090-2104}}, keywords = {{mass; spectrometry; surface plasmon resonance; SCP-domain; protein complex; prostate cancer; seminal plasma; PSP94; cysteine-rich secretory protein; beta-microseminoprotein}}, language = {{eng}}, number = {{2}}, pages = {{555--561}}, publisher = {{Elsevier}}, series = {{Biochemical and Biophysical Research Communications}}, title = {{beta-Microseminoprotein binds CRISP-3 in human seminal plasma}}, url = {{http://dx.doi.org/10.1016/j.bbrc.2005.05.139}}, doi = {{10.1016/j.bbrc.2005.05.139}}, volume = {{333}}, year = {{2005}}, }