Abstract
The pioneering work of Munn and colleagues (Munn and Greville, 1969) was the first tangible indication that the larvae of holometabolous insects synthesize large amounts of unusual proteins which accumulate in their hemolymph. These proteins, generally referred to as larval serum proteins (LSPs) or storage proteins, have many common characteristics. They are synthesized by the fat body of actively feeding larvae and their concentrations increase enormously in the last larval instar, making up the major component of the whole larval soluble proteins. They form hexamers in the 5 × 105 Dalton range and dissociate into polypeptides of 7.2 – 9 × 104 Daltons (For review, see Levenbook, 1985). Telfer et al. (1983) suggested that the larval haemolymph proteins which are similar in structure and amino acid composition to calliphorin, the major haemolymph protein of the blowfly, Calliphora vicina, should be called arylphorins to signify that they bear aryl groups.
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Scheller, K., Fischer, B., Schenkel, H. (1990). Molecular Properties, Functions and Developmentally Regulated Biosynthesis of Arylphorin in Calliphora vicina . In: Hagedorn, H.H., Hildebrand, J.G., Kidwell, M.G., Law, J.H. (eds) Molecular Insect Science. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-3668-4_19
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