@article{oai:obihiro.repo.nii.ac.jp:00000280,
 author = {Nozaki, Hirofumi and Miyamoto, Akio and 宮本, 明夫 and Hayashi, Ken-go and Matsui, Motozumi and 松井, 基純 and Yoshida, Takashi and Nakamura, Tadashi and Arai, Ikichi and 荒井, 威吉 and Urashima, Tadasu and 浦島, 匡},
 issue = {4},
 journal = {Journal of Applied Glycoscience},
 month = {},
 note = {application/pdf, 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.},
 pages = {315--320},
 title = {N-Acetylglucosaminyltransferase I Activity in Bovine Ovarian Follicular Fluids from Dominant and Atretic Follicles},
 volume = {51},
 year = {2004}
}