[The immunochemical detection of apoprotein dissociation from particles of very low-density lipoproteins in human blood plasma].
The dissociation of very-low-density lipoprotein (VLDL) apoproteins was studied using immunochemical approaches. The analysis of monospecific antibody binding to apo E, C-II and C-III on VLDL surface showed low apoprotein accessibility for the antibodies while the accessibility of apo C-II and C-III in solution was complete. Lipoprotein preparation dilution resulted in increasing of apo E and C-II accessibility. It was suggested that apoprotein dissociation led to apoprotein cluster dissolving on VLDL surface and higher antigen determinant accessibility. The findings confirmed previous theoretical analysis of apoprotein dissociation.
Shuvaev
V V
VV
Dergunov
A D
AD
Perova
N V
NV
D000818:Animals; D000906:Antibodies / Q000097:blood / Q000302:isolation & purification; D001059:Apoproteins / Q000097:blood* / Q000276:immunology; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D005454:Fluorescence Polarization; D006801:Humans; D007114:Immunization; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D008079:Lipoproteins, VLDL / Q000097:blood* / Q000276:immunology; D011485:Protein Binding; D011817:Rabbits; D012996:Solutions; D013499:Surface Properties
D000906:Antibodies; D001059:Apoproteins; D007140:Immunoglobulin Fab Fragments; D008079:Lipoproteins, VLDL; D012996:Solutions
Immunokhimicheskoe obnaruzhenie otdeleniia apobelkov ot chastits lipoproteinov ochen' nizkoĭ plotnosti plazmy krovi cheloveka.