Linked Life Data

6812653

Source:http://linkedlifedata.com/resource/pubmed/id/6812653

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1982-12-16
pubmed:abstractText
A simple method for determination of lysine residue number and positive charge of histones H1 and H5 in the acetic acid -- urea system has been developed. The method is based on incomplete succinylation of lysine residues and allows an accurate determination of protein molecular length. The accuracy of the method has been demonstrated by determination of goose and chicken histones H5 and their fragments. The calibrating curve for determination of molecular lengths of histones H1 and H5 has been plotted. Using the incomplete succinylation method, a detailed analysis of Lymantria dispar histone H1 structure has been carried out. The method under discussion can be used for determining lysine residue number, positive charge and molecular length of practically any protein.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1378-85
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
[Determination of lysine residue number, positive charge and molecular lengths of histone H1 and H5 by a method of incomplete succinylation].
pubmed:publicationType
Journal Article, English Abstract