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Clones for rat hepatic lipase were isolated by probing a rat liver cDNA library in lambda gt11 with an oligonucleotide synthesized on the basis of a partial peptide sequence. The cloned messenger codes for a protein of 472 amino acids plus a hydrophobic leader sequence of 22 amino acids. The unglycosylated protein has a predicted molecular weight of 53,222 and contains two potential sites for N-glycosylation. The protein bears striking regions of homology with other known lipases and contains peptide sequences that have been implicated in lipid binding. The homologous mRNA is present in liver tissue but no detectable mRNA is observed in the adrenal gland, despite the reported presence of hepatic lipase in both the liver and the adrenal gland. No mRNA was seen in any of a variety of other tissues.
Komaromy et al. (Sun,) studied this question.