The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase
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...
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ndltd-bl.uk-oai-ethos.bl.uk-5003512017-06-27T03:37:33ZThe functional characterisation of the acidic domain of N-Arginine Dibasic ConvertaseSingleton, Kirsty2009N-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.572.76Glasgow Caledonian Universityhttp://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.500351Electronic Thesis or Dissertation |
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572.76 Singleton, Kirsty The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase |
description |
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. |
author |
Singleton, Kirsty |
author_facet |
Singleton, Kirsty |
author_sort |
Singleton, Kirsty |
title |
The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase |
title_short |
The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase |
title_full |
The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase |
title_fullStr |
The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase |
title_full_unstemmed |
The functional characterisation of the acidic domain of N-Arginine Dibasic Convertase |
title_sort |
functional characterisation of the acidic domain of n-arginine dibasic convertase |
publisher |
Glasgow Caledonian University |
publishDate |
2009 |
url |
http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.500351 |
work_keys_str_mv |
AT singletonkirsty thefunctionalcharacterisationoftheacidicdomainofnargininedibasicconvertase AT singletonkirsty functionalcharacterisationoftheacidicdomainofnargininedibasicconvertase |
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1718466155977375744 |