지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국식품영양과학회 Journal of Food Science and Nutrition Journal of Food Science and Nutrition Vol.4 No.2
- 발행연도
- 1999.6
- 수록면
- 145 - 151 (7page)
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초록· 키워드
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Apolipoprotein B-100 (apo B-100) is an important component in plasma low density lipoproteins (LDL). It functions as the ligand for the LDL receptor in peripheral cells. The LDLs are removed from the circulation by both high-affinity receptor-mediated and receptor-independant pathways. LDLs are heterogeneous in their lipid content, size and density and certain LDL subspecies increase risk of atherosclerosis due to differences in the conformation of apo B in the particle. In the present study, surface and core peptide fraction of Apo B-100 have been characterized by comparing peptide-mapping and fluorescence spectroscopy. Surface fragments of apo B-100 were generated by digestion of LDL with either trypsin, pronase, or pancreatic elastase. Surface fractions were fractionated on a Sephadex G-50 column. The remaining core fragments were delipidated and redigested with the above enzymes, and the resulting core peptides were compared with surface peptides. Results from peptide-mapping by HPLC showed pronase-digestion was more extensive than trypsin-digestion to remove surface peptide fraction from LDL. Fluorescence spectra showed that core fractions contained higher amount of tryptophan than surface fractions, and it indicated that core fraction was more hydrophobic than surface fractions. A comparison of the behavior of the core and surface provided informations about the regions of apo B-100 involved in LDL metabolism and also about the structural features concerning the formation of atherosclerosis.
목차
Abstract
INTRODUCTION
MATERIALS AND METHODS
RESULTS AND DISCUSSION
REFERENCES
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