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In vitro studies of the interaction of isolated Lp(a) lipoprotein and other serum lipoproteins with glycosaminoglycans
Author(s) -
Dahlén G.,
Ericson C.,
Berg K.
Publication year - 1978
Publication title -
clinical genetics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 102
eISSN - 1399-0004
pISSN - 0009-9163
DOI - 10.1111/j.1399-0004.1978.tb02058.x
Subject(s) - glycosaminoglycan , lipoprotein , lipoprotein(a) , chemistry , divalent , in vitro , plasma protein binding , biochemistry , sepharose , binding site , cholesterol , enzyme , organic chemistry
The interaction of isolated Lp(a) lipoprotein or other lipoprotein classes with different glycosaminoglycans (GAG) bound to activated Sepharose was studied. In contrast to LDL, the Lp(a) lipoprotein did not bind to the GAG tested if sodium was used as a buffer cation. In the presence of Ca ++ , however, even the Lp(a) lipoprotein was bound to GAG. This type of binding, probably mediated by divalent cation bridges, is apparently not a simple function of the GAG used. Addition of GAG in solution revealed that this binding, as well as the binding in the absence of Ca ++ , is reversible. The Ca ++ mediated binding may be the only one existing under physiological conditions, and it appears possible that the Lp(a) lipoprotein is bound more firmly to GAG than is LDL under such conditions.