Disulfide pairings and secondary structure of porcine β-microseminoprotein

Iren Wang, Tsun Ai Yu, Shih Hsiung Wu, Wen Chang Chang, Chinpan Chen

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine β-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The five disulfide pairings on porcine MSP were unambiguously assigned based on NMR data and further confirmed using structural calculations. Surprisingly, our derived pairings differ from those recently reported for ostrich MSP based on matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis. Furthermore, the secondary structure was determined to comprise one four-stranded and two double-stranded antiparallel β-sheets. As we know, this is the first detailed secondary structure reported among several types of MSPs.

Original languageEnglish
Pages (from-to)80-84
Number of pages5
JournalFEBS Letters
Issue number1-3
Publication statusPublished - Apr 24 2003
Externally publishedYes


  • Human prostate secretory protein of 94 amino acids
  • Na,K-adenosine triphosphatase inhibitor
  • Nuclear magnetic resonance
  • Structure
  • β-Microseminoprotein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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