beta-Microseminoprotein binds CRISP-3 in human seminal plasma

Summary, in English

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.

• Författare: L Udby; Åke Lundwall; A H Johnsen; Per Fernlund; Camilla Valtonen-André; Anna Blom; Hans Lilja; N Borregaard; L Kieldsen; Anders Bjartell
• Avdelning/ar: Klinisk kemi, Malmö; Institutionen för translationell medicin; Urologisk cancerforskning, Malmö
• Publiceringsår: 2005
• Språk: Engelska
• Sidor: 555-561
• Publikation/Tidskrift/Serie: Biochemical and Biophysical Research Communications
• Volym: 333
• Issue: 2
• Länkar: http://dx.doi.org/10.1016/j.bbrc.2005.05.139
• Dokumenttyp: Artikel i tidskrift
• Förlag: Elsevier
• Ämne: Biological Sciences
• Nyckelord: mass; spectrometry; surface plasmon resonance; SCP-domain; protein complex; prostate cancer; seminal plasma; PSP94; cysteine-rich secretory protein; beta-microseminoprotein
• Status: Published
• Forskningsgrupp: Clinical Chemistry, Malmö; Urological cancer, Malmö
• ISBN/ISSN/Övrigt: ISSN: 1090-2104