|
rdf:type |
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|
lifeskim:mentions |
|
|
pubmed:issue |
6
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|
pubmed:dateCreated |
1977-5-20
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pubmed:abstractText |
The L-asparagine analogue 5-diazo-4-oxo-L-[5-14C]norvaline binds irreversibly to the active site of Escherichia coli L-asparaginase. Conditions for optimal labeling in buffers containing 50% dimethylsulfoxide have been developed and kinetic parameters of the inactivation have been determined. After reduction, alkylation and subsequent degradation of the modified enzyme with alpha-chymotrypsin, the principal radioactive decapeptide of sequence Val-Gly-Ala-Met-Arg-Pro-Ser-Thr-Ser-Met was isolated. A second radioactive hexapeptide Arg-Pro-Ser-Thr-Ser-Met resulting from chymotryptic digestion of the decapeptide was also isolated. Evidence is presented for the attachment of the 5-diazo-4-oxo-L-norvaline residue to serine-9 in the decapeptide via an acid-labile linkage.
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pubmed:language |
eng
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pubmed:journal |
|
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
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|
pubmed:day |
25
|
|
pubmed:volume |
252
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2072-6
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|
pubmed:dateRevised |
2009-10-27
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pubmed:meshHeading |
|
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pubmed:year |
1977
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|
pubmed:articleTitle |
Structure of peptide from active site region of Escherichia coli L-asparaginase.
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|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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