Purification and Primary StructureDetermination of Human LysosomalDipeptidase

Verfasser / Beitragende:
[I. Dolenc, M. Mihelič]
Ort, Verlag, Jahr:
2003
Enthalten in:
Biological Chemistry, 384/2(2003-02-20), 317-320
Format:
Artikel (online)
ID: 378874284
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024 7 0 |a 10.1515/BC.2003.036  |2 doi 
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245 0 0 |a Purification and Primary StructureDetermination of Human LysosomalDipeptidase  |h [Elektronische Daten]  |c [I. Dolenc, M. Mihelič] 
520 3 |a 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. 
540 |a Copyright © 2003 by Walter de Gruyter GmbH & Co. KG 
690 7 |a Biochemistry  |2 nationallicence 
690 7 |a Molecular biology  |2 nationallicence 
690 7 |a Cellular biology  |2 nationallicence 
700 1 |a Dolenc  |D I.  |4 aut 
700 1 |a Mihelič  |D M.  |4 aut 
773 0 |t Biological Chemistry  |d Walter de Gruyter  |g 384/2(2003-02-20), 317-320  |x 1431-6730  |q 384:2<317  |1 2003  |2 384  |o bchm 
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950 |B NATIONALLICENCE  |P 773  |E 0-  |t Biological Chemistry  |d Walter de Gruyter  |g 384/2(2003-02-20), 317-320  |x 1431-6730  |q 384:2<317  |1 2003  |2 384  |o bchm 
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