Abstract
Quantitative determination of proteins was made by a new immunoelectrophoresis technique in which tubular canals are partly filled with agarose gel containing antibodies. The procedure is simple and practicable. Sample volumes of a few .mu.l up to several hundred .mu.l may be added for each test. The amount of protein in a sample was linearly related to the distance from the point of application (i.e., gel surface) to the front of the immunoprecipitation zone. The zone immunoelectrophoresis method shows the following advantages over rocket immunoelectrophoresis: less consumption of antibodies, much lower detection limit (0.05 .mu.g protein/ml) and larger concentration range with a linear calibration curve. A high correlation (0.98) between the 1st- and last-mentioned method was obtained for .alpha.1-antitrypsin. Precision data are given for albumin and .alpha.-fetoprotein, and typically a relative SD of a few percent was obtained.

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