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( Masaru Murata ),( Toshiyuki Akazawa ),( Junichi Hino ),( Junichi Tazaki ),( Katsutoshi Ito ),( Makoto Arisue ),( Maxillofacial Surgery ) 조선대학교 치의학연구원 2011 Oral Biology Research (Oral Biol Res) Vol.35 No.1
The aim of this study was to evaluate the hard tissue-inductive capability by human decalcified dentin matrix (DDM) with or without recombinant human bone morphogenetic protein-2 (BMP-2). Human teeth were crushed, completely decalcified and freeze-dried. We named the material DDM. The shape of DDM was a particle type and its size varied from 0.4 to 0.8 mm. The hard tissue induction by 70 mg of DDM was estimated histologically in the nude mice subcutaneous tissue at 4 weeks after implantation. The DDM alone induced bone and cartilage, independently, in the back skin. In addition, the time-course of bone induction by BMP-2 (5.0 μg)/DDM (70 mg) was analyzed in the rat subcutaneous tissues. Histological findings showed that the BMP-2/DDM induced bone and marrow between the DDM particles. Calcium content in the BMP-2/DDMinduced tissue was compatible to the histological findings. The morphometric analysis demonstrated that the BMP-2/DDM showed 66.9%, 79.0% in the volume of bone and marrow, and 32.4%, 21.0% in that of DDM at 8, 32 weeks, respectively. These results indicate that human DDM particles are osteo-chondroinductive and absorbable matrics. Human DDM are effective biomaterials of BMP-2 delivering for bone engineering.
Akihiro Morio,Jian Xu,Akitsu Masuda,Yurie Kinoshita,Masato Hino,Daisuke Morokuma,Hatsumi M. Goda,Nozomu Okino,Makoto Ito,Hiroaki Mon,Ryosuke Fujita,Takahiro Kusakabe,이재만 한국응용곤충학회 2019 Journal of Asia-Pacific Entomology Vol.22 No.2
The O-glycosidase, endo-α-N-acetylgalactosaminidase from Enterococcus faecalis (endoEF) catalyzes the cleavage of core 1 and core 3 type O-linked disaccharides between GalNAc and serine or threonine residues from glycoproteins. The endoEF has broad substrate specificity and thus is extensively utilized for the structural and functional analysis of the O-linked glycans. In this study, we expressed and purified the recombinant endoEF (rEndoEF) by using the silkworm-baculovirus expression vector system (Silkworm-BEVS) and confirmed the deglycosylation activity of rEndoEF targeting reporter glycoproteins, which was equivalent to the commercial Oglycosidase. Thus, our study provides important clues to produce highly active rEndoEF O-glycosidases employing silkworm-BEVS as an alternative.