caa a22 4500 378874284 CHVBK 20180305123416.0 cr unu---uuuuu 161128e20030220xx s 000 0 eng 10.1515/BC.2003.036 doi (NATIONALLICENCE)gruyter-10.1515/BC.2003.036 Purification and Primary StructureDetermination of Human LysosomalDipeptidase [Elektronische Daten] [I. Dolenc, M. Mihelič] The lysosomal metallopeptidase is an enzyme that acts preferentially on dipeptides with unsubstituted N- and C-termini. Its activity is highest in slightly acidic pH. Here we describe the isolation and characterization of lysosomal dipeptidase from human kidney. The isolated enzyme has the amino-terminal sequence DVAKAIINLAVY and is a homodimer with a molecular mass of 100 kDa. So far no amino acid sequence has been determined for this metallopeptidase. The complete primary structure as deduced from the nucleotide sequence revealed that the isolated dipeptidase is similar to blood plasma glutamate carboxypeptidase. Copyright © 2003 by Walter de Gruyter GmbH & Co. KG Biochemistry nationallicence Molecular biology nationallicence Cellular biology nationallicence Dolenc I. aut Mihelič M. aut Biological Chemistry Walter de Gruyter 384/2(2003-02-20), 317-320 1431-6730 384:2<317 2003 384 bchm https://doi.org/10.1515/BC.2003.036 text/html Onlinezugriff via DOI 1 research article jats NATIONALLICENCE 856 40 https://doi.org/10.1515/BC.2003.036 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Dolenc I. aut NATIONALLICENCE 700 1- Mihelič M. aut NATIONALLICENCE 773 0- Biological Chemistry Walter de Gruyter 384/2(2003-02-20), 317-320 1431-6730 384:2<317 2003 384 bchm CC0 http://creativecommons.org/publicdomain/zero/1.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-gruyter