Cloning and Sequence Analyses of cDNAs Encoding Aminoacylase I from Porcine Kidney
- 1 January 1992
- journal article
- Published by Walter de Gruyter GmbH in Biological Chemistry Hoppe-Seyler
- Vol. 373 (2) , 1227-1232
- https://doi.org/10.1515/bchm3.1992.373.2.1227
Abstract
CDNAs encoding L-aminoacylase (EC 3.5.1.14) were isolated from a lambda gt10 cDNA library derived from porcine kidney mRNA. The clones were identified by hybridization with a synthetic oligonucleotide probe based on partial peptide sequences, or with a DNA probe encoding human aminoacylase I. Several cDNA clones isolated from the library had a length of about 1.3 kbp. They contained an open reading frame of 1218 bp encoding a polypeptide of 406 amino acids. The deduced amino-acid sequence contains the known peptide sequences; in addition, M(r) (45.3 kDa) and amino-acid composition of the predicted polypeptide match those of purified aminoacylase I. Data base searches did not reveal significant sequence homologies of aminoacylase I with other well-known amidases.Keywords
This publication has 5 references indexed in Scilit:
- Aminoacylase I is not a glycolipid-anchored ectoenzyme in pig kidneyBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Monoclonal Antibody Based Immunoassay for Human Aminoacylase-1Journal of Immunoassay, 1989
- Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parametersBiochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1988
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982
- Ueber Spaltungen und Synthesen im ThierkörperNaunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie, 1881