Use this URL to cite or link to this record in EThOS: | https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.500351 |
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Title: | The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase | ||||
Author: | Singleton, Kirsty |
ISNI:
0000 0004 2672 4402
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Awarding Body: | Glasgow Caledonian University | ||||
Current Institution: | Glasgow Caledonian University | ||||
Date of Award: | 2009 | ||||
Availability of Full Text: |
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Abstract: | |||||
N-Aiginine Dibasic Convertase (NRD-C) is a prohormone convertase purified and cloned from rat testis. NRD-C is classified within the zinc metalloprotease family of proteases of which other members include Pitrilysin and Insulysin. NRD-C is a MOkDa protein predominantly located within the testes but is also present at lower levels in other endocrine systems such as the cortex and adrenal glands. NRD-C functions to cleave peptide sequences on the N-terminal of an arginine residue in a pair of basic amino acids. Cleavage by NRD-C is highly specific. In order to elucidate the function of the acidic domain of NRD-C the following specific project aims are proposed: study possible protein-protein interactions within the'acidic domain using a yeast-two-hybrid approach and examine whether the acidic domain affects the cellular localisation of the enzyme using green fluorescent protein NRD-C chimeric proteins.
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Supervisor: | Not available | Sponsor: | Not available | ||
Qualification Name: | Thesis (Ph.D.) | Qualification Level: | Doctoral | ||
EThOS ID: | uk.bl.ethos.500351 | DOI: | Not available | ||
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