|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0002518,
umls-concept:C0010511,
umls-concept:C0031727,
umls-concept:C0033684,
umls-concept:C0043393,
umls-concept:C0047701,
umls-concept:C0205102,
umls-concept:C0205132,
umls-concept:C0337112,
umls-concept:C0449830,
umls-concept:C0486805,
umls-concept:C0678594,
umls-concept:C0728938,
umls-concept:C0936012,
umls-concept:C1305923,
umls-concept:C1514562,
umls-concept:C1524075,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2603343
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|
pubmed:issue |
3
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pubmed:dateCreated |
1981-12-21
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pubmed:abstractText |
The purpose of this work was to contribute to the study of the covalent structure of yeast 3-phosphoglycerate kinase. First, we undertook the complete alignment of the four fragments produced by cyanogen-bromide cleavage and which constitute the intact protein; we then established the total amino acid sequence of a 30-residue peptide and the N-terminal sequence of a 65-residue peptide. Second, we analyzed the acetylated state of the protein. The analyses of the acid fraction "P" obtained after digestion of 3-phosphoglycerate kinase by pronase enabled us to determine the N-terminal sequence of this enzyme as N-acetylserylglycine. Third, we isolated, purified and analyzed seven tryptic peptides from a fragment containing 102 amino acids coming from the N-terminal end of the protein. The peptides occupying the N- and C-terminal ends of this fragment were also identified.
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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:month |
Mar
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pubmed:issn |
0367-8377
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
17
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
393-400
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
|
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pubmed:year |
1981
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pubmed:articleTitle |
Structural studies on yeast 3-phosphoglycerate kinase. Linear arrangement of the CNBr fragments, partial amino acid sequence of the inner part of the polypeptide chain, and analyses of the N-terminal domain of the protein.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
