Earticle

초록

영어

The pattern analysis of glycosylation sites is a promising strategy to distinguish the recombination enzyme for the enzyme replacement therapy (ERT) from the native human. Cerezyme is a glycoprotein that has studied for treatment of Gaucher disease. Gaucher disease, the most common lysosomal storage disease, is caused by results of mutations of glucocerebrosidase(GC) which dissolves glucocerebroside. Most patients who suffer from Gaucher disease takes the enzyme replacement therapy (ERT) with imiglucerase, cerezyme(R). The recombinant imiglucocerase must be required as enzyme similar to the native human enzyme sequence. The glycosylation patterns of recombinant imiglucocerase simultaneously should be analogous to those of the native human enzyme. However, the analysis of glycosylation patterns shows that the structure of glycans in recombinant imiglucocerase is similar, but distinct from those of glycans in the native human enzyme. The glycosylation sites of the recombinant enzyme must be consistent with those of the native human enzyme. The patterns of glycopeptides must be characterized in order to identify the glycosylation sites of glycoproteins. Here, we present the glycosylation sites of the imiglucocerease (cerezyme(R)) using MALDI-TOF MS.

저자

• Sang Jin Park [ Biotechnology Fusion Research Team, Division of Life Science, Korea Basic Science Institute, Daejeon ]
• Sun Mi Park [ Biotechnology Fusion Research Team, Division of Life Science, Korea Basic Science Institute, Daejeon ]
• Jun Mi Lee [ Biotechnology Fusion Research Team, Division of Life Science, Korea Basic Science Institute, Daejeon ]
• Kyung-Bok Lee [ Biotechnology Fusion Research Team, Division of Life Science, Korea Basic Science Institute, Daejeon ]
• Soohyun Kim [ Biotechnology Fusion Research Team, Division of Life Science, Korea Basic Science Institute, Daejeon ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국당과학회 학술대회

• 간기

  연간

• 수록기간

  2006~2022

• 십진분류

  KDC 517 DDC 614