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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1980-8-28
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pubmed:abstractText |
An improved method is described for the preparation of milligram quantities of substrate-modified sulphatase A. The latter has the same molecular weight and the same ability to form a tetramer as has native sulphatase A. It has been shown that the modified enzyme prepared with nitrocatechol [35S]sulphate as substrate contains 1 mol 35SO24- per mol enzyme and that any treatment which causes reversion of the modified enzyme to native enzyme is accompanied by the loss of the bound SO24-. Dialysis of the 35S-modified enzyme against a solution containing SO24- causes a loss of 35SO24- with no change in the amount of modified enzyme in the preparation. It has been shown that the activation of the substrate-modified enzyme by SO24- does not lead to the formation of a third stable form of sulphatase A.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
613
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
130-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7378414-Animals,
pubmed-meshheading:7378414-Arylsulfatases,
pubmed-meshheading:7378414-Catechols,
pubmed-meshheading:7378414-Cattle,
pubmed-meshheading:7378414-Chemical Phenomena,
pubmed-meshheading:7378414-Chemistry,
pubmed-meshheading:7378414-Drug Stability,
pubmed-meshheading:7378414-Enzyme Activation,
pubmed-meshheading:7378414-Kinetics,
pubmed-meshheading:7378414-Liver,
pubmed-meshheading:7378414-Molecular Weight,
pubmed-meshheading:7378414-Spectrophotometry, Ultraviolet,
pubmed-meshheading:7378414-Sulfatases,
pubmed-meshheading:7378414-Sulfates
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pubmed:year |
1980
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pubmed:articleTitle |
The sulphatase of ox liver. XXIII. The nature of substrate-modified sulphatase A.
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pubmed:publicationType |
Journal Article
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