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Title: Amino-acid sequence and tissue distribution of guinea-pig leukotriene A4 hydrolase. Author: Minami M, Mutoh H, Ohishi N, Honda Z, Bito H, Shimizu T. Journal: Gene; 1995 Aug 19; 161(2):249-51. PubMed ID: 7665088. Abstract: The guinea-pig leukotriene A4 hydrolase (LTA4H)-encoding cDNA was isolated from a guinea-pig lung cDNA library by cross-hybridization using a human probe. The deduced amino acid (aa) sequence consists of 611 aa (68 756 Da) and contains all twelve internal peptide and N-terminal sequences determined from the purified enzyme from guinea-pig intestine. The aa identity of the guinea-pig enzyme with its human, mouse and rat counterparts was 92.9, 90.5 and 90.4%, respectively. The previously characterized zinc-binding motif and a putative active site were highly conserved, supporting the aminopeptidase activity described for this enzyme. RNA blot analysis demonstrated ubiquitous expression of the LTA4H mRNA.[Abstract] [Full Text] [Related] [New Search]