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Nucleic Acids Research, 1985, Vol. 13, No. 6 1891-1903
© 1985

Articles

Molecular cloning and nucleotide sequence of rat lingual lipase cDNA

A.J.P. Docherty*, M.W. Bodmer, S. Angal1, R. Verger2, C. Riviere2, P.A. Lowe1, A. Lyons, J.S. Emtage and T.J.R. Harris

Department of Molecular Biology 244-250 Bath Road, Slough, SL1 4DY, UK 1Protein Biochemistry, Celltech Limited 244-250 Bath Road, Slough, SL1 4DY, UK 2Center de Biochimie et Biologie Moleculaire du CNRS 31 Chemin Joseph Aiguier, Marseille 9, France

*To whom reprint requests should be sent

Received January 10, 1985. Revised February 28, 1985. Accepted February 28, 1985.

Purified rat lingual lipase (EC3113), a glycoprotein of approximate molecular weight 52,000, was used to generate polyclonal antibodies which were able to recognise the denatured and deglycosylated enzyme. These immunoglobulins were used to screen a cDNA library prepared from mRNA isolated from the serous glands of rat tongue cloned in E. coli expression vectors. An almost full length cDNA clone was isolated and the nucleotide and predicted amino acid sequence obtained. Comparison with the N-terminal amino acid sequence of the purified enzyme confirmed the identity of the cDNA and indicated that there was a hydrophobic signal sequence of 18 residues. The amino acid sequence of mature rat lingual lipase consists of 377 residues and shares little hamology with porcine pancreatic lipase apart fran a short region containing a serine residue at an analogous position to the ser 152 of the porcine enzyme.


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