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Clinical Chemistry 31: 1654-1658, 1985;
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Clinical Chemistry, Vol 31, 1654-1658, Copyright © 1985 by American Association for Clinical Chemistry

Monoclonal antibodies can precipitate low-density lipoprotein. I. Characterization and use in determining apolipoprotein B [published erratum appears in Clin Chem 1986 Feb;32(2):390]

S Marcovina, D France, RA Phillips and SJ Mao

We produced 20 mouse monoclonal antibodies against human plasma low- density lipoprotein (LDL). Individually they failed to precipitate LDL in agarose gel by the double-immunodiffusion technique; collectively they did, or as few as two combined monoclonal antibodies could do so. To mimic polyclonal antibodies in determination of apolipoprotein B (apo B) by radial immunodiffusion, a combination of four particular monoclonal antibodies (clones A, B, C, and D) was necessary. We characterized these four clones with respect to temperature dependency, affinity, total binding to 125I-labeled LDL, and specificity to the different species of apolipoprotein B. Two monoclonal antibodies (B and C) bound 100% of 125I-labeled LDL; clones A and D bound 80% and 87%, respectively. All four clones bound maximally to LDL at 4 degrees C. The affinity constants for clones A, B, C, and D were 0.6, 2.1, 3.8, and 2.3 X 10(9) L/mol, respectively. By the Western blotting technique, the four monoclonal antibodies all reacted with the species B-100 and B- 74 of apolipoprotein B, and to various degrees with B-48 and B-26. Radial immunodiffusion (chi) and direct enzyme-linked immunosorbent assay (y) with a mixture of the four monoclonal antibodies gave almost identical results for 70 patients: y = 0.921 chi-2.58; r = 0.933.


The following articles in journals at HighWire Press have cited this article:


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 J DAIRY SCIHome page
W. L. Chen, M. T. Huang, H. C. Liu, C. W. Li, and S. J. T. Mao
Distinction Between Dry and Raw Milk Using Monoclonal Antibodies Prepared Against Dry Milk Proteins
J Dairy Sci, August 1, 2004; 87(8): 2720 - 2729.
[Abstract] [Full Text] [PDF]


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