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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1987 Oct;84(19):6677–6681. doi: 10.1073/pnas.84.19.6677

Molecular cloning and amino acid sequence of leukotriene A4 hydrolase.

C D Funk 1, O Rådmark 1, J Y Fu 1, T Matsumoto 1, H Jörnvall 1, T Shimizu 1, B Samuelsson 1
PMCID: PMC299146  PMID: 2821541

Abstract

A cDNA clone corresponding to leukotriene A4 hydrolase was isolated from a human lung lambda gt11 expression library by immunoscreening with a polyclonal antiserum. Several additional clones from human lung and placenta cDNA lambda g11 libraries were obtained by plaque hybridization with the 32P-labeled lung cDNA clone. One of these clones has an insert of 1910 base pairs that contains the complete protein-coding region. From the deduced primary structure, leukotriene A4 hydrolase is a 610 amino and protein with a calculated molecular weight of 69,140. No apparent homologies with microsomal epoxide hydrolases were found. RNA blot analysis indicated substantial amounts of a discrete mRNA of approximately equal to 2250 nucleotides in lung tissue and leukocytes.

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Selected References

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