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L-Canavanine competes with L-arginine for incorporation into vitellogenin secreted in vitro by the fat body of the female locust Locusta migratoria migratorioides. Incorporation of L-[guanidinooxy-14C]canavanine into vitellogenin has been established unequivocally by combined arginase and urease hydrolyses of the acid hydrolysate of antibody-precipitated canavanyl vitellogenin. Continued exposure of the fat body to canavanine decreases in vitro protein secretion but the proportion of canavanyl vitellogenin to native vitellogenin increases. Canavanine-mediated inhibition of fat body protein secretion is dependent on both the canavanine concentration and the arginine retention by the fat body. Canavanine replaces about 10% of the arginyl residues of canavanyl vitellogenin. The electrophoretic mobility of canavanyl vitellogenin is greater than that of native vitellogenin but the ability of this aberrant protein to react with vitellogenin antibody is unimpaired.

In vitro incorporation of L-canavanine into vitellogenin of the fat body of the migratory locust Locusta migratoria migratorioides.