A new membrane-associated Ca2+-binding protein of rat spermatogenic cells: Its purification and characterization

Masahisa Nakamura*, Tomoyo Yamanobe, Takashi Suyemitsu, Masayuki Komukai, Ryuichi Kan, Shoichi Okinaga, Kiyoshi Arai

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


A Ca2+-binding protein of Mr=52000, estimated by SDS-PAGE, was purified to a final yield of 0.04% from rat spermatogenic cells. Purification steps included gel filtration, ammonium sulfate precipitation and HPLC. Amino acid analysis showed the content of 34% acidic residues and 15% basic residues. The isoelectric point of this protein was 4.7. Dot-blot analysis indicated that the Ca2+-binding protein bound 2 mol of calcium per mol of protein. This protein had two binding sites with dissociation constants of 4.8 μM and 0.2 μM. No appreciable amount of hexose was observed (<1 μg of hexose/70 ug of protein). This protein may play an important role such as the Ca2+-transport in the plasma membrane of spermatogenic cells.

Original languageEnglish
Pages (from-to)1358-1364
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 1991 May 15
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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