Linked Life Data

8389548

Source:http://linkedlifedata.com/resource/pubmed/id/8389548

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-7-2
pubmed:abstractText
In the presence of sodium dodecyl sulfate and 2-mercaptoethanol, the human papillomavirus 16 E7 protein migrates as a 17 kD protein during polyacrylamide gel electrophoresis. However, the theoretical molecular mass of this protein is approximately 11 kD. Substitution of 2 basic amino acids for 2 acidic residues in the amino terminus of the protein restored normal electrophoretic mobility. Furthermore, neutralization of negative charge through chemical modification of the wild type protein normalized migration. These results indicate that the substantial net negative charge of the wild type E7 protein is responsible for its anomalous electrophoretic behavior.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
192
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1380-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The anomalous electrophoretic behavior of the human papillomavirus type 16 E7 protein is due to the high content of acidic amino acid residues.
pubmed:affiliation
Department of Microbiology and Immunology, Indiana University School of Medicine, Indianapolis 46202-5120.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't