Abstract
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 language | English |
|---|---|
| Pages (from-to) | 1358-1364 |
| Number of pages | 7 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 176 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - 1991 May 15 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
A new membrane-associated Ca2+-binding protein of rat spermatogenic cells : Its purification and characterization. / Nakamura, Masahisa; Yamanobe, Tomoyo; Suyemitsu, Takashi; Komukai, Masayuki; Kan, Ryuichi; Okinaga, Shoichi; Arai, Kiyoshi.
In: Biochemical and Biophysical Research Communications, Vol. 176, No. 3, 15.05.1991, p. 1358-1364.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A new membrane-associated Ca2+-binding protein of rat spermatogenic cells
T2 - Its purification and characterization
AU - Nakamura, Masahisa
AU - Yamanobe, Tomoyo
AU - Suyemitsu, Takashi
AU - Komukai, Masayuki
AU - Kan, Ryuichi
AU - Okinaga, Shoichi
AU - Arai, Kiyoshi
PY - 1991/5/15
Y1 - 1991/5/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0025820680&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0025820680&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(91)90436-B
DO - 10.1016/0006-291X(91)90436-B
M3 - Article
C2 - 2039518
AN - SCOPUS:0025820680
VL - 176
SP - 1358
EP - 1364
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -