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Storage proteins of the fall webworm, Hyphantria cunea drury
Author(s) -
Kim Hak Ryul,
Kang C. S,
Mayer Richard T.
Publication year - 1989
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.940100203
Subject(s) - hyphantria , hemolymph , biology , storage protein , instar , vitellogenin , larva , pupa , botany , biochemistry , gene
Two storage proteins, storage protein‐1 (SP1) and storage protein‐2 (SP2), were found in hemolymph and fat body during the development of Hyphantria cunea , the fall webworm. Both storage proteins show similiar quantitative changes during development in males and females; however, SP1 is more abundant. The hemolymph of last instar larvae contains high concentrations of the storage proteins. However, following pupation, the storage proteins accumulate in fat bodies. SP1 peaks in the hemolymph of males and females late in last instar larvae (8‐day‐old 7th instar larvae). SP1 has a native molecular weight of 460,000 and consists of six identical subunits (Mr = 76,700), while SP2 has a molecular weight of 450,000 and is composed of two different subunits (Mr = 74,100 and 72,400). Both SP1 and SP2 are hexamers and are phosphorylated glycolipoproteins. The pl values of SP1 and SP2 were determined to be 5.70 and 5.50, respectively. Antibodies raised against SP1 react positively with vitellogenin and ovary extract, as well as with proteins in the hemolymph from last instar larvae and proteins in pupal fat bodies. Storage protein synthesis starts in fat bodies of a 4‐day‐old 7th instar larvae and in female peaks at 6–8 days of the 7th instar.