Sequence of a 17 kDa vacuolar H(+)-ATPase proteolipid subunit from insect midgut and Malpighian tubules. Academic Article

abstract

• A 0.4 kb polymerase chain reaction (PCR) product obtained from cDNA made from the midgut and Malpighian tubules of fifth instar larvae of Heliothis virescens was used to screen a larval midgut and Malpighian tubules cDNA library. Four clones were obtained, one of 1.9 kb and others of 1.4 kb. The 1.9 kb clone encodes a 17.2 kDa protein which is highly homologous to other vacuolar ATPases proteolipids. Putative N-glycosylation and DCCD binding sites were observed at amino acid residues 83 and 139, respectively.

authors

• Pietrantonio, Patricia

published proceedings

• Insect Biochem Mol Biol

author list (cited authors)

• Pietrantonio, P. V., & Gill, S. S.

citation count

• 7

complete list of authors

• Pietrantonio, PV||Gill, SS

publication date

• January 1993

publisher

• Elsevier  Publisher

published in

• Insect Biochemistry and Molecular Biology  Journal

keywords

• Amino Acid Sequence
• Animals
• Base Sequence
• Cloning, Molecular
• Digestive System
• Larva
• Malpighian Tubules
• Molecular Sequence Data
• Moths
• Proteolipids
• Proton-translocating Atpases
• Sequence Homology, Amino Acid
• Vacuoles

Digital Object Identifier (DOI)

• 10.1016/0965-1748(93)90041-p

start page

• 675

end page

• 680

volume

• 23

issue

• 6

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2F0965-1748%2893%2990041-p