| Literature DB >> 2764915 |
J Ishizaki1, O Ohara, E Nakamura, M Tamaki, T Ono, A Kanda, N Yoshida, H Teraoka, H Tojo, M Okamoto.
Abstract
Based on the partial amino acid sequences of membrane-associated phospholipase A2 (PLA2M), belonging to group II, purified from rat spleen, the cDNA encoding PLA2M was cloned by a new cloning strategy utilizing enzymatic cDNA amplification. At the N-terminus of the coded 146 residues, which were deduced from the cDNA sequence, the putative signal peptide was found despite the tight adherence of this enzyme to the membrane. The sequence of rat PLA2M exhibits 75% homology with that of human group II PLA2 in the protein-coding region. The result of RNA blot analysis showed that rat ileal mucosa contains the largest amount of the PLA2 transcript among the tissues examined.Entities:
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Year: 1989 PMID： 2764915 DOI： 10.1016/0006-291x(89)90777-8
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575