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

• Published in: Biochimica et biophysica acta Vol. 1351; no. 1; pp. 42 - 46
• Main Authors: Nittoh, Takeaki, Hirakata, Mikito, Mue, Suetsugu, Ohuchi, Kazuo
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 20.03.1997
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Blood Proteins - genetics; cDNA cloning; Cloning, Molecular; DNA, Complementary - genetics; Eosinophil; Eosinophil cationic protein; Eosinophil Granule Proteins; Eosinophil-associated ribonuclease; Eosinophils - enzymology; Molecular Sequence Data; PCR; Polymerase Chain Reaction; Rapid amplification of cDNA ends; Rat; Rats; Ribonucleases - genetics; RNase; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Rat; EAR, eosinophil-associated ribonuclease; p I, isoelectric point; Eosinophil; Eosinophil-associated ribonuclease; cDNA, complementary deoxyribonucleic acid; MBP, major basic protein; cDNA cloning; RNase, ribonuclease; PCR, polymerase chain reaction; RACE, rapid amplification of cDNA ends; Eosinophil cationic protein; ECP, eosinophil cationic protein; EDN, eosinophil-derived neurotoxin; Rapid amplification of cDNA ends; PCR; RNase
• ISSN: 0167-4781; 0006-3002; 1879-2634
• DOI: 10.1016/S0167-4781(97)00024-9

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%). © 1997 Elsevier Science B.V. All rights reserved.