In:
European Journal of Biochemistry, Wiley, Vol. 79, No. 1 ( 1977-09), p. 259-264
Abstract:
A comparison of the ionization behaviour of the human apoA‐II, apoC‐I, apoC‐III proteins and of their complexes with dimyristoyl lecithin is based on potentiometric titration of the basic and acidic residues and spectrophotometric titration of the phenolic groups. Experimental data suggest that a number of lysine, arginine, aspartic acid and glutamic acid residues are masked in the complexes. For each of these amino acids and in all three proteins the number of masked residues is consistent with the content of those regions predicted to be involved in lipid binding by the model of Segrest et al. [ FEBS Lett. 38 , 247–253 (1974)]. These data taken together with the results of calo‐rimetric and titration experiments with the apoA‐I protein reported in the accompanying article [Rosseneu et al. (1977) Eur. J. Biochem. 79 , 251–257] strongly support the general na ture of the proposed model and further suggest that ionic interactions have some role in the formation of the dimyristoyl lecithin/apolipoprotein complexes.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1977.79.issue-1
DOI:
10.1111/j.1432-1033.1977.tb11804.x
Language:
English
Publisher:
Wiley
Publication Date:
1977
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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