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Insect Biochemistry
Pines, M., Department of Entomology, The Hebrew University, Rehovot, 76100, Israel
Applebaum, S.W., Department of Entomology, The Hebrew University, Rehovot, 76100, Israel
Locust fat body protein kinase is dependent on, and maximally stimulated by 5 × 10-6 M cyclic GMP and to a lesser extent by cyclic AMP. It exhibits a pH optimum of 6.9, an unusual requirement for high Mg2+ (maximum at 100 mM) or an alternative requirement for Mn2+ (maximum at 5 mM). Maximal stimulation by Mg2+ is twice that by Mn2+. Rabbit muscle protein kinase inhibitor uncharacteristically inhibits both cyclic AMP and cyclic GMP stimulated protein kinase activity of locust fat body, the former 5-fold more than the latter, with histone IIA as acceptor. The degree of phosphorylation differs for different acceptor proteins: histone IIA > locust vitellin > arginine-rich histone. Casein is barely phosphorylated and bovine serum albumin (fraction V) not at all. The high threshold for Mg2+ activation may be related to the high levels of Mg2+ in locust haemolymph, to the preferential phosphorylation of vitellin, and to the fact that the fat body is the site of vitellogenin synthesis. © 1978.
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Cyclic nucleotide-dependent protein kinase activity of adult female locust fat body
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Pines, M., Department of Entomology, The Hebrew University, Rehovot, 76100, Israel
Applebaum, S.W., Department of Entomology, The Hebrew University, Rehovot, 76100, Israel
Cyclic nucleotide-dependent protein kinase activity of adult female locust fat body
Locust fat body protein kinase is dependent on, and maximally stimulated by 5 × 10-6 M cyclic GMP and to a lesser extent by cyclic AMP. It exhibits a pH optimum of 6.9, an unusual requirement for high Mg2+ (maximum at 100 mM) or an alternative requirement for Mn2+ (maximum at 5 mM). Maximal stimulation by Mg2+ is twice that by Mn2+. Rabbit muscle protein kinase inhibitor uncharacteristically inhibits both cyclic AMP and cyclic GMP stimulated protein kinase activity of locust fat body, the former 5-fold more than the latter, with histone IIA as acceptor. The degree of phosphorylation differs for different acceptor proteins: histone IIA > locust vitellin > arginine-rich histone. Casein is barely phosphorylated and bovine serum albumin (fraction V) not at all. The high threshold for Mg2+ activation may be related to the high levels of Mg2+ in locust haemolymph, to the preferential phosphorylation of vitellin, and to the fact that the fat body is the site of vitellogenin synthesis. © 1978.
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