Purification and localization of a calcium-binding protein in human spermatozoa

Masahisa Nakamura; Hiromichi Ishikawa; Kouhei Matsuda; Teruaki Iwamoto; Seiji Furuya; Tomoyo Yamanobe; Masayuki Komukai; Kazutoshi Yamamoto; Akihiro Tamura; Shoichi Okinaga; Kiyoshi Arai

Purification and localization of a calcium-binding protein in human spermatozoa

Masahisa Nakamura^*, Hiromichi Ishikawa, Kouhei Matsuda, Teruaki Iwamoto, Seiji Furuya, Tomoyo Yamanobe, Masayuki Komukai, Kazutoshi Yamamoto, Akihiro Tamura, Shoichi Okinaga, Kiyoshi Arai

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

The purpose of this study was to purify a calcium-binding protein (CalBP) from human spermatozoa of 226 men and to determine the localization of this protein in spermatozoa. The sperm cells were extracted with 0.6 MKCI, and the KCI extract was then subjected to gel filtration and high performance liquid chromatography. Two CalBPs of M_r = 38 kDa and 52 kDa were found by ⁴⁵Ca²⁺-binding on blotted proteins. Only a 52 kDa CalBP (CalBP-52) was purified to a final yield of 0.007%. The isoelectric point of this protein was 5.1. The human CalBP-52 reacted with rabbit antiserum directed against rat 52 kDa CalBP. An immuno-cytochemical study showed that this protein was localized on the sperm head. It is postulated that this protein may have important functions related to Ca²⁺-transport into sperm cells.

Original language	English
Pages (from-to)	500-505
Number of pages	6
Journal	Human Reproduction
Volume	7
Issue number	4
Publication status	Published - 1992 Apr
Externally published	Yes

Keywords

CalBP-52
Human
Spermatozoa

ASJC Scopus subject areas

Statistics, Probability and Uncertainty
Applied Mathematics
Physiology (medical)
Reproductive Medicine
Obstetrics and Gynaecology
Rehabilitation
Developmental Biology
Physiology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Cite this

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title = "Purification and localization of a calcium-binding protein in human spermatozoa",

abstract = "The purpose of this study was to purify a calcium-binding protein (CalBP) from human spermatozoa of 226 men and to determine the localization of this protein in spermatozoa. The sperm cells were extracted with 0.6 MKCI, and the KCI extract was then subjected to gel filtration and high performance liquid chromatography. Two CalBPs of Mr = 38 kDa and 52 kDa were found by 45Ca2+-binding on blotted proteins. Only a 52 kDa CalBP (CalBP-52) was purified to a final yield of 0.007%. The isoelectric point of this protein was 5.1. The human CalBP-52 reacted with rabbit antiserum directed against rat 52 kDa CalBP. An immuno-cytochemical study showed that this protein was localized on the sperm head. It is postulated that this protein may have important functions related to Ca2+-transport into sperm cells.",

keywords = "CalBP-52, Human, Spermatozoa",

author = "Masahisa Nakamura and Hiromichi Ishikawa and Kouhei Matsuda and Teruaki Iwamoto and Seiji Furuya and Tomoyo Yamanobe and Masayuki Komukai and Kazutoshi Yamamoto and Akihiro Tamura and Shoichi Okinaga and Kiyoshi Arai",

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T1 - Purification and localization of a calcium-binding protein in human spermatozoa

AU - Nakamura, Masahisa

AU - Ishikawa, Hiromichi

AU - Matsuda, Kouhei

AU - Iwamoto, Teruaki

AU - Furuya, Seiji

AU - Yamanobe, Tomoyo

AU - Komukai, Masayuki

AU - Yamamoto, Kazutoshi

AU - Tamura, Akihiro

AU - Okinaga, Shoichi

AU - Arai, Kiyoshi

PY - 1992/4

Y1 - 1992/4

N2 - The purpose of this study was to purify a calcium-binding protein (CalBP) from human spermatozoa of 226 men and to determine the localization of this protein in spermatozoa. The sperm cells were extracted with 0.6 MKCI, and the KCI extract was then subjected to gel filtration and high performance liquid chromatography. Two CalBPs of Mr = 38 kDa and 52 kDa were found by 45Ca2+-binding on blotted proteins. Only a 52 kDa CalBP (CalBP-52) was purified to a final yield of 0.007%. The isoelectric point of this protein was 5.1. The human CalBP-52 reacted with rabbit antiserum directed against rat 52 kDa CalBP. An immuno-cytochemical study showed that this protein was localized on the sperm head. It is postulated that this protein may have important functions related to Ca2+-transport into sperm cells.

AB - The purpose of this study was to purify a calcium-binding protein (CalBP) from human spermatozoa of 226 men and to determine the localization of this protein in spermatozoa. The sperm cells were extracted with 0.6 MKCI, and the KCI extract was then subjected to gel filtration and high performance liquid chromatography. Two CalBPs of Mr = 38 kDa and 52 kDa were found by 45Ca2+-binding on blotted proteins. Only a 52 kDa CalBP (CalBP-52) was purified to a final yield of 0.007%. The isoelectric point of this protein was 5.1. The human CalBP-52 reacted with rabbit antiserum directed against rat 52 kDa CalBP. An immuno-cytochemical study showed that this protein was localized on the sperm head. It is postulated that this protein may have important functions related to Ca2+-transport into sperm cells.

KW - CalBP-52

KW - Human

KW - Spermatozoa

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C2 - 1522193

AN - SCOPUS:0026529461

SN - 0268-1161

VL - 7

SP - 500

EP - 505

JO - Human Reproduction

JF - Human Reproduction

IS - 4

ER -

Purification and localization of a calcium-binding protein in human spermatozoa

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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