SECONDARY STRUCTURE OF THE PARTICLE ASSOCIATING DOMAIN OF APOLIPOPROTEIN-B-100 IN LOW-DENSITY-LIPOPROTEIN BY ATTENUATED TOTAL-REFLECTION INFRARED-SPECTROSCOPY

被引:47
|
作者
GOORMAGHTIGH, E [1 ]
CABIAUX, V [1 ]
DEMEUTTER, J [1 ]
ROSSENEU, M [1 ]
RUYSSCHAERT, JM [1 ]
机构
[1] ST JAN HOSP,BRUGGE,BELGIUM
关键词
D O I
10.1021/bi00074a023
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The secondary structure of the human low-density lipoprotein (LDL) apo B-100 fragment embedded in the lipid domain of the particle has been investigated by Fourier transform attenuated total reflection infrared spectroscopy (FTIR-ATR). The solvent-exposed region of the protein was hydrolyzed by using different proteases (alpha-chymotrypsin, trypsin, proteinase K) for incubation times varying between 24 min and 48 h. Analysis of the FTIR-ATR spectra after repurification of the digested LDL particle indicates the same trend for all the hydrolysis conditions tested: the peptides remaining associated with the particle are rich in beta-sheet structure. Dichroism spectra reveal that at least part of the beta-sheets is associated with the phospholipid component of the particle.
引用
收藏
页码:6104 / 6110
页数:7
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