Pv. Pietrantonio et Ss. Gill, SEQUENCE OF A 17 KDA VACUOLAR H-ATPASE PROTEOLIPID SUBUNIT FROM INSECT MIDGUT AND MALPIGHIAN TUBULES(), Insect biochemistry and molecular biology, 23(6), 1993, pp. 675-680
A 0.4 kb polymerase chain reaction (PCR) product obtained from cDNA ma
de from the midgut and Malpighian tubules of fifth instar larvae of He
liothis virescens was used to screen a larval midgut and Malpighian tu
bules cDNA library. Four clones were obtained, one of 1.9 kb and other
s of 1.4 kb. The 1.9 kb clone encodes a 17.2 kDa protein which is high
ly homologous to other vacuolar ATPases proteolipids. Putative N-glyco
sylation and DCCD binding sites were observed at amino acid residues 8
3 and 139, respectively.