期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 333, 期 2, 页码 555-561出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2005.05.139
关键词
cysteine-rich secretory protein; beta-microseminoprotein; PSP94; seminal plasma; prostate cancer; protein complex; SCP-domain; mass spectrometry; surface plasmon resonance
资金
- NCI NIH HHS [P50 CA092629, P50-CA92629] Funding Source: Medline
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. (c) 2005 Elsevier Inc. All rights reserved.
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