β-Microseminoprotein binds CRISP-3 in human seminal plasma

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-co...

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Bibliographic Details
Main Authors: Udby, L, Lundwall, Å, Johnsen, A, Fernlund, P, Valtonen-André, C, Blom, A, Lilja, H, Borregaard, N, Kjeldsen, L, Bjartell, A
Format: Journal article
Language:English
Published: 2005
Description
Summary: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.