Efficient translation of long-lived messengers in extracts from dry pea primary axes

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Abstract
Extracts prepared from dry pea (Pisum sativum, L; cv oberon) primary axes translate efficiently their endogenous messengers in an in vitro protein synthesizing system. The native long-lived messengers are biologically fully active and direct the synthesis of a whole range of polypeptides with MW ranging up to 130,000. About 0.5% of the total in vitro synthesized polypeptides are recovered in the immunoprecipitate obtained with pea lectin antiserum. Since about one-fourth of the radioactivity in the immunoprecipitate comigrates with authentic pea lectin it is concluded that about 0.1% of the long-lived messengers code for the lectin.