Data/hora: 11/06/2024 07:22:22

Provedor de dados: 	19	
País: 	Japan	
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	
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.	
Data: 	2004	
Ano: 	2004	
Palavras-chave: 	N-acetylglucosaminyltransferase I; Dominant follicle; Atretic follicle; Follicular fluid; Bovine.	
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&gt; α1-3α1-6 mannotriose&gt;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.	
Idioma: 	Inglês	
Identificador: 	http://ir.obihiro.ac.jp/dspace/handle/10322/4185	
Editor: 	日本応用糖質科学会	
Fonte: 	日本応用糖質科学会