T. Nittoh et al., IDENTIFICATION OF CDNA FOR RAT HOMOLOGS OF HUMAN MAJOR BASIC-PROTEIN AND EOSINOPHIL CATIONIC PROTEIN, International archives of allergy and immunology, 117, 1998, pp. 5-9
We have determined the complete nucleotide sequence for cDNA of rat ho
mologues of human eosinophil major basic protein (MBP) and eosinophil
cationic protein (ECP) using the rapid amplification of cDNA ends (RAC
E) procedure. Nucleotide sequence of cDNA of rat MBP revealed that mRN
A of rat MBP encodes a protein containing 227 amino acids which has th
ree functional domains; namely, the signal peptide, the acidic peptide
that contains numerous acidic amino acids and the mature MBP, as in h
uman, guinea pig and mouse MBP. In addition, cDNA of a rat homologue o
f human ECP was also cloned. The deduced amino acid sequence revealed
that this gene encodes a putative protein with a molecular weight of 1
5.5 kD which has ribonuclease activity. The homology of amino acid seq
uence between the rat homologue and the murine eosinophil-associated r
ibonucleases (EARs) was high (65%). Therefore, we named this rat homol
ogue 'rat EAR-1'.