β-Microseminoprotein binds CRISP-3 in human seminal plasma

Journal article

β-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 aminoterminal SCP-domain. © 2005 Elsevier Inc. All rights reserved.

Authors: Udby, L; Lundwall, Å; Johnsen, A; Fernlund, P; Valtonen-André, C

• Journal: Biochemical and Biophysical Research Communications
• Volume: 333
• Issue: 2
• Pages: 555-561
• Publication date: 2005-07-29
• DOI: 10.1016/j.bbrc.2005.05.139
• ISSN: 0006-291X
• Language: English
• Keywords: Cysteine-rich secretory protein; Mass spectrometry; SCP-domain; Prostate cancer; Seminal plasma; Protein complex; β-Microseminoprotein; Surface plasmon resonance; PSP94