期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1981
卷号：78
期号：9
页码：5480-5483
DOI：10.1073/pnas.78.9.5480
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
