Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-6-10
pubmed:abstractText
Two forms of liver metallothioneins (MTs) were purified from hedgehog exposed to zinc, using gel filtration on Sephacryl S-100 and DEAE Sepharose Fast Flow chromatography. The peptide chain weight of both MT-1 and MT-2 was found to be about 10,000, as determined by high performance liquid chromatography. This value was higher than that calculated from amino acid analysis. The amino acid composition of hedgehog liver MT-1 and MT-2 resembles that of liver to MTs from rabbit and other species. Their distinctive features include an extremely high cysteine content, about 33% of all the amino acid residues, and an absence of aromatic amino acids and histidine. In addition, a rapid method for the determination of MTs during animal tissue purification has been established. The samples were directly added in an ammoniacal solution of a Co(II) salt for recording linear sweep polarograms. By comparison with the commonly used metal determination method, our method is direct, rapid, credible and suitable for all the MTs or MT-like samples.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0269-3879
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
94-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Purification and characterization of hedgehog liver metallothioneins.
pubmed:affiliation
Department of Biology, Peking University, Beijing, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't