The use of anti-immunoglobulin for the immunoprecipitation of labeled proteins from tissue homogenates

Amnon Hizi*, Gad Yagil

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

An improved immunochemical procedure for the quantitative isolation of labeled minor proteins from tissue homogenates is worked out and is applied to the isolation of glucose-6-phosphate dehydrogenase from mouse liver. Goat anti-enzyme serum is used as primary reagent, followed by rabbit anti-goat IgG, and not by carrier enzyme as in currently used methods. The resulting immunoprecipitates are analyzed by acrylamide gel electrophoresis, so that only counts in enzyme bands are registered. An equivalent precipitate formed with serum from nonimmunized goat serves as an efficient control for coprecipitation.

Original languageEnglish
Pages (from-to)386-399
Number of pages14
JournalAnalytical Biochemistry
Volume62
Issue number2
DOIs
StatePublished - Dec 1974
Externally publishedYes

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