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Identification of cDNA encoding rat eosinophil cationic protein/eosinophil-associated ribonuclease

descriptionPublicationkeyboard_double_arrow_right Article 01 Mar 1997 English Publisher:Elsevier BVJournal:Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, volume 1,351, pages 42-46 (issn: 0167-4781,

Authors: Suetsugu Mue; Takeaki Nittoh; Mikito Hirakata; Kazuo Ohuchi;

doi: 10.1016/s0167-4781(97)00024-9

pmid: 9116043

Identification of cDNA encoding rat eosinophil cationic protein/eosinophil-associated ribonuclease

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Abstract

Using the rapid amplification of cDNA ends (RACE) procedure, we have determined the complete nucleotide sequence for the cDNA encoding rat eosinophil cationic protein (ECP)/eosinophil-associated ribonuclease (EAR). The deduced amino acid sequence revealed that the molecular weight of rat preECP/EAR is 18.0 kDa and the isoelectric point is 9.85, indicating that rat ECP/EAR is highly cationic. The homology of amino acid sequence between rat ECP/EAR and human ECP is 54%, and that between rat ECP/EAR and human eosinophil-derived neurotoxin (EDN) is 51%. Rat ECP/EAR is also homologous to human ribonuclease k6 (homology 47%).

Related Organizations

Tohoku University
Japan

Keywords

DNA, Complementary, Base Sequence, Sequence Homology, Amino Acid, Molecular Sequence Data, Blood Proteins, Sequence Analysis, DNA, Eosinophil Granule Proteins, Polymerase Chain Reaction, Rats, Eosinophils, Ribonucleases, Animals, Amino Acid Sequence, Cloning, Molecular

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