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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1979-9-1
pubmed:abstractText
Horseradish peroxidase (HRP), a glycoprotein enzyme, bound specifically to Mallory bodies (MBs) in cryostat sections of autopsy liver and liver biopsies. In contrast, HRP did not bind to cryostat sections of normal liver. The specificity of HRP binding was also observed using light and electron microscopy in autopsy liver-derived subcell fractions prepared by the MB isolation procedure. In order to quantitate HRP binding, a solid phase colorimetric assay was developed. This assay involves immobilizing purified MBs or homogenized tissue fractions in glass tubes, incubating with HRP, and measuring the enzymatic activity of bound HRP. A linear relationship between MB concentration and HRP binding was observed. The assay was capable of detecting as little as 1 microgram of MB protein. The specificity of HRP binding was also investigated using the solid phase assay. The specific activity (HRP bound per milligram of protein) of purified MBs was 10 to 15 times that of a glass wool-filtered liver homogenate suggesting that the solid phase assay may be of use in monitoring the purification of MBs. HRP did not bind to normal liver homogenate even when large loads were assayed. The results of this study indicate that HRP binding, employed cytochemically, represents a rapid and facile procedure for ascertaining the presence of MBs in tissue. In some cases, those structures may not be easily visualized by conventional staining procedures. Furthermore, quantitation of MBs in tissue may be possible by using a solid phase enzyme-linked assay.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0023-6837
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Mallory bodies. Horseradish peroxidase: specific cytochemical and biochemical marker for alcoholic hyalin.
pubmed:publicationType
Journal Article