| Registro completo |
| Provedor de dados: |
OAK
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| País: |
Japan
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| Título: |
ウシ優性卵胞と閉鎖卵胞の卵胞液中におけるN-アセチルグルコサミニルトランスフェラーゼ I 活性の解析
N-Acetylglucosaminyltransferase I Activity in Bovine Ovarian Follicular Fluids from Dominant and Atretic Follicles
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| Autores: |
Nozaki, Hirofumi
Miyamoto, Akio
Hayashi, Ken-Go
Matsui, Motozumi
Yoshida, Takashi
Nakamura, Tadashi
Arai, Ikichi
Urashima, Tadasu
宮本, 明夫
松井, 基純
中村, 正
浦島, 匡
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| Data: |
2004
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| Ano: |
2004
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| Palavras-chave: |
N-acetylglucosaminyltransferase I
Dominant follicle
Atretic follicle
Follicular fluid
Bovine
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| Resumo: |
The activity of α3-D-mannoside-β-1,2-N-acetylglucosaminyltransferase I (GnT I; EC 2.4.1.101), which catalyzes the first step in the conversion of oligomannose to complex or hybrid N-glycans of glycoproteins, was detected in bovine follicular fluid (bFF). The GnT I activity in bFF had a pH optimum of 5.8 and an absolute requirement for either Co2+, Mn2+, or Mg2+, the activity being stimulated by these cations in the above order. The apparent Km value for α1-3α1-6 mannopentaose of GnT I in bFF was 2.17 mM. The substrate specificity for the GnT I activity decreased in the following order: α1-3α1-6 mannopentaose> α1-3α1-6 mannotriose>α1-3 mannobiose. The GnT I activity in bFF from large atretic follicles was significantly higher than in that from large dominant follicles. Moreover there was no significant difference between the GnT I activities in bFF from dominant follicles collected before and after surge of luteinizing hormone (LH surge). These data suggest that the GnT I activity in bFF may reflect functional changes in the microenvironment which lead to follicular atresia.
https://www.jstage.jst.go.jp/article/jag/51/4/51_4_315/_article
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| Idioma: |
Inglês
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| Identificador: |
http://ir.obihiro.ac.jp/dspace/handle/10322/4185
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| Editor: |
日本応用糖質科学会
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| Direitos: |
日本応用糖質科学会
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