Earticle

현재 위치 Home

Poster-23

Quantitative Analysis of Glycan Microarrays for Assaying Galactosyltransferase Activity

첫 페이지 보기
  • 발행기관
    한국당과학회 바로가기
  • 간행물
    한국당과학회 학술대회 바로가기
  • 통권
    2008 Eastern Asian Glycoscience Symposium (2008.11)바로가기
  • 페이지
    pp.72-73
  • 저자
    Sungjin Park,, Injae Shin
  • 언어
    영어(ENG)
  • URL
    https://www.earticle.net/Article/A192360

※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.

원문정보

초록

영어
Glycan microarrays have been used recently as an advanced technology for the high-throughput analysis of protein-carbohydrate interactions and for the detection of cells and pathogens. A major driving force behind the expanded use of this microarray technology is the development of new experimental protocols in which they can be applied. As a continuous effort to extend the use of this technology, carbohydrate microarrays were applied for assaying glycosyltransferase activities. The microarray-based approach requires only a small amount of immobilized acceptor substrates (picomoles), and enzymatic catalytic activities are facilely analyzed by measuring the amount of a product formed in a time-dependent manner. The level of time-dependent product conversion is determined by using fluorescence detection of lectin recognition of carbohydrate products. Carbohydrate microarrays immobilized twenty glycan probes were prepared by immobilizing hydrazide-conjugated carbohydrates on epoxide-coated glass slides. Treatment of glycan microarrays with β-1,4-galactosyltransferase in the presence of UDP-Gal and Mn2+ showed that α- and β-GlcNAc were converted to α- and β-LacNAc, respectively. In addition, this experiment indicated that β-GlcNAc was a better substrate than α-GlcNAc for this enzyme, which was also confirmed by HPLC analysis of enzymatic product of each substrate and solution-based assay. Furthermore, quantitative binding affinities (Kd values) between α-LacNAc or β-LacNAc and RCA120 were determined by using carbohydrate microarrays. The Kd values (34 nM for α-LacNAc and 33 nM for β-LacNAc) determined from carbohydrate microarrays were similar to those (26.3 nM for α-LacNAc and 25.3 nM for β-LacNAc) obtained by using a conventional SPR technology. These findings should open new applications of carbohydrate microarrays in the field of glycomics research.

저자

  • Sungjin Park, [ Department of Chemistry, Yonsei University ]
  • Injae Shin [ Department of Chemistry, Yonsei University ]

참고문헌

자료제공 : 네이버학술정보

간행물 정보

발행기관

  • 발행기관명
    한국당과학회 [Korean Society for Glycoscience]
  • 설립연도
    2006
  • 분야
    의약학>약학
  • 소개
    본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.

간행물

  • 간행물명
    한국당과학회 학술대회
  • 간기
    연간
  • 수록기간
    2006~2022
  • 십진분류
    KDC 517 DDC 614

이 권호 내 다른 논문 / 한국당과학회 학술대회 2008 Eastern Asian Glycoscience Symposium

    피인용수 : 0(자료제공 : 네이버학술정보)

    함께 이용한 논문 이 논문을 다운로드한 분들이 이용한 다른 논문입니다.

      페이지 저장