Purification and characterization of cathepsin D from herring muscle ( Clupea harengus )
Cathepsin D was purified and concentrated 469-fold from a homogenate of Clupea harengus muscle. The purified enzyme is a monomer with a molecular weight of 38 000-39 000. It is inhibited by pepstatin and has optimal activity at pH 2.5 with hemoglobin as the substrate. The isoelectric point is at pH...
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ftdtupubl:oai:pure.atira.dk:publications/9cdcf5b6-c22e-48cb-9304-8fcb16c90bf8 2024-04-28T07:58:28+00:00 Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) Nielsen, L.B. Nielsen, Henrik Hauch 2001 https://orbit.dtu.dk/en/publications/9cdcf5b6-c22e-48cb-9304-8fcb16c90bf8 eng eng https://orbit.dtu.dk/en/publications/9cdcf5b6-c22e-48cb-9304-8fcb16c90bf8 info:eu-repo/semantics/restrictedAccess Nielsen , L B & Nielsen , H H 2001 , ' Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) ' , Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology , vol. 128B , no. 2 , pp. 351-363 . Råvare- og produktteknologi article 2001 ftdtupubl 2024-04-03T14:47:44Z Cathepsin D was purified and concentrated 469-fold from a homogenate of Clupea harengus muscle. The purified enzyme is a monomer with a molecular weight of 38 000-39 000. It is inhibited by pepstatin and has optimal activity at pH 2.5 with hemoglobin as the substrate. The isoelectric point is at pH 6.8. Glycosidase treatment and binding to Concanavalin A indicated that the enzyme contains one N-linked carbohydrate moiety of the high-mannose type per molecule. The first 21 amino acid residues of the N-terminal showed high similarity to cathepsin D from antarctic icefish liver (Chionodraco hamatus) and trout ovary (Oncorhynchus mykiss). Digestion of the P-chain of oxidized insulin resulted in preferential cleavage at Leu(15)-Tyr(16), (47%), Tyr(16)-Leu(17) (34%) and Ala(14)- Leu(15) (18%). Incubation with myofibrils from herring muscle at pH 4.23 showed that the enzyme mainly degraded myosin, actin and tropomyosin. (C) 2001 Elsevier Science Inc. All rights reserved. Article in Journal/Newspaper Antarc* Antarctic Icefish Technical University of Denmark: DTU Orbit |
institution |
Open Polar |
collection |
Technical University of Denmark: DTU Orbit |
op_collection_id |
ftdtupubl |
language |
English |
topic |
Råvare- og produktteknologi |
spellingShingle |
Råvare- og produktteknologi Nielsen, L.B. Nielsen, Henrik Hauch Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) |
topic_facet |
Råvare- og produktteknologi |
description |
Cathepsin D was purified and concentrated 469-fold from a homogenate of Clupea harengus muscle. The purified enzyme is a monomer with a molecular weight of 38 000-39 000. It is inhibited by pepstatin and has optimal activity at pH 2.5 with hemoglobin as the substrate. The isoelectric point is at pH 6.8. Glycosidase treatment and binding to Concanavalin A indicated that the enzyme contains one N-linked carbohydrate moiety of the high-mannose type per molecule. The first 21 amino acid residues of the N-terminal showed high similarity to cathepsin D from antarctic icefish liver (Chionodraco hamatus) and trout ovary (Oncorhynchus mykiss). Digestion of the P-chain of oxidized insulin resulted in preferential cleavage at Leu(15)-Tyr(16), (47%), Tyr(16)-Leu(17) (34%) and Ala(14)- Leu(15) (18%). Incubation with myofibrils from herring muscle at pH 4.23 showed that the enzyme mainly degraded myosin, actin and tropomyosin. (C) 2001 Elsevier Science Inc. All rights reserved. |
format |
Article in Journal/Newspaper |
author |
Nielsen, L.B. Nielsen, Henrik Hauch |
author_facet |
Nielsen, L.B. Nielsen, Henrik Hauch |
author_sort |
Nielsen, L.B. |
title |
Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) |
title_short |
Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) |
title_full |
Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) |
title_fullStr |
Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) |
title_full_unstemmed |
Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) |
title_sort |
purification and characterization of cathepsin d from herring muscle ( clupea harengus ) |
publishDate |
2001 |
url |
https://orbit.dtu.dk/en/publications/9cdcf5b6-c22e-48cb-9304-8fcb16c90bf8 |
genre |
Antarc* Antarctic Icefish |
genre_facet |
Antarc* Antarctic Icefish |
op_source |
Nielsen , L B & Nielsen , H H 2001 , ' Purification and characterization of cathepsin D from herring muscle ( Clupea harengus ) ' , Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology , vol. 128B , no. 2 , pp. 351-363 . |
op_relation |
https://orbit.dtu.dk/en/publications/9cdcf5b6-c22e-48cb-9304-8fcb16c90bf8 |
op_rights |
info:eu-repo/semantics/restrictedAccess |
_version_ |
1797569735288684544 |