Purification and Primary StructureDetermination of Human LysosomalDipeptidase
Gespeichert in:
Verfasser / Beitragende:
[I. Dolenc, M. Mihelič]
Ort, Verlag, Jahr:
2003
Enthalten in:
Biological Chemistry, 384/2(2003-02-20), 317-320
Format:
Artikel (online)
Online Zugang:
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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 | |
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| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Dolenc |D I. |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Mihelič |D M. |4 aut | ||
| 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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