Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.

Purine nucleoside phosphorylase was isolated and purified from cell extracts of Proteus vulgaris recovered from spoiling cod fish (Gadus morhua). The molecular weight and isoelectric point of the enzyme were 120,000 +/- 2,000 and pH 6.8. The Michaelis constant for inosine as substrate was 3.9 x 10(-...

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Main Authors: Surette, M, Gill, T, MacLean, S
Format: Text
Language:English
Published: 1990
Subjects:
Research Article
Gadus morhua
Online Access:http://www.ncbi.nlm.nih.gov/pmc/articles/PMC184424
http://www.ncbi.nlm.nih.gov/pubmed/2111121
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spelling ftpubmed:oai:pubmedcentral.nih.gov:184424 2023-05-15T16:19:02+02:00 Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris. Surette, M Gill, T MacLean, S 1990-05 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC184424 http://www.ncbi.nlm.nih.gov/pubmed/2111121 en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC184424 http://www.ncbi.nlm.nih.gov/pubmed/2111121 Research Article Text 1990 ftpubmed 2013-08-29T13:26:08Z Purine nucleoside phosphorylase was isolated and purified from cell extracts of Proteus vulgaris recovered from spoiling cod fish (Gadus morhua). The molecular weight and isoelectric point of the enzyme were 120,000 +/- 2,000 and pH 6.8. The Michaelis constant for inosine as substrate was 3.9 x 10(-5). Guanosine also served as a substrate (Km = 2.9 x 10(-5). However, the enzyme was incapable of phosphorylizing adenosine. Adenosine proved to be useful as a competitive inhibitor and was used as a ligand for affinity chromatography of purine nucleoside phosphorylase following initial purification steps of gel filtration and ion-exchange chromatography. Text Gadus morhua PubMed Central (PMC)
institution Open Polar
collection PubMed Central (PMC)
op_collection_id ftpubmed
language English
topic Research Article
spellingShingle Research Article
Surette, M
Gill, T
MacLean, S
Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
topic_facet Research Article
description Purine nucleoside phosphorylase was isolated and purified from cell extracts of Proteus vulgaris recovered from spoiling cod fish (Gadus morhua). The molecular weight and isoelectric point of the enzyme were 120,000 +/- 2,000 and pH 6.8. The Michaelis constant for inosine as substrate was 3.9 x 10(-5). Guanosine also served as a substrate (Km = 2.9 x 10(-5). However, the enzyme was incapable of phosphorylizing adenosine. Adenosine proved to be useful as a competitive inhibitor and was used as a ligand for affinity chromatography of purine nucleoside phosphorylase following initial purification steps of gel filtration and ion-exchange chromatography.
format Text
author Surette, M
Gill, T
MacLean, S
author_facet Surette, M
Gill, T
MacLean, S
author_sort Surette, M
title Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
title_short Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
title_full Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
title_fullStr Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
title_full_unstemmed Purification and characterization of purine nucleoside phosphorylase from Proteus vulgaris.
title_sort purification and characterization of purine nucleoside phosphorylase from proteus vulgaris.
publishDate 1990
url http://www.ncbi.nlm.nih.gov/pmc/articles/PMC184424
http://www.ncbi.nlm.nih.gov/pubmed/2111121
genre Gadus morhua
genre_facet Gadus morhua
op_relation http://www.ncbi.nlm.nih.gov/pmc/articles/PMC184424
http://www.ncbi.nlm.nih.gov/pubmed/2111121
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