Document Detail


Isolation and characterization of six human hepatic isometallothioneins.
MedLine Citation:
PMID:  4062903     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human hepatic metallothionein (MT) was separated into six isoforms by using reversed-phase h.p.l.c. at the analytical and preparative levels. By comparison with the h.p.l.c. elution profiles of the charge-separable species MT-1 and MT-2 isolated by the procedure of Bühler & Kägi [(1974) FEBS Lett. 39, 229-234], five of these isoproteins are identified as hitherto unresolved subforms of MT-1, and one is identical with MT-2. The six isoforms have distinct and reproducible retention times at neutral pH, where the metal remains bound to the protein, and at low pH, where the metal is removed. Their amino acid compositions display the high cysteine content and the lack of aromatic amino acids and of histidine typical of mammalian metallothioneins, but they differ significantly with respect to all other amino acids. A survey of autopsy material indicates that in adult human liver all six isoforms are usually expressed, albeit in somewhat variable relative proportions.
Authors:
P E Hunziker; J H Kägi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Biochemical journal     Volume:  231     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1985 Oct 
Date Detail:
Created Date:  1985-12-19     Completed Date:  1985-12-19     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  375-82     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / analysis
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Humans
Liver / analysis*
Metallothionein / isolation & purification*
Chemical
Reg. No./Substance:
0/Amino Acids; 9038-94-2/Metallothionein
Comments/Corrections

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