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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.

Original publication

DOI

10.1016/j.bbrc.2005.05.139

Type

Journal article

Journal

Biochemical and Biophysical Research Communications

Publication Date

29/07/2005

Volume

333

Pages

555 - 561