Abstract:
:Rabbit antisera specific for horseradish peroxidase inhibit the catalytic activity of the enzyme. All antibodies prepared against the holoenzyme react with the peroxidase apoenzyme. However, only a minority (30-45%) of the total antiperoxidase pool cross react with reduced and alkylated apoenzymes. The antibodies inhibiting peroxidase activity do not bind to S-carboxymethyl of S-carboxamidomethylated apoenzyme derivatives as measured by absorption and competition of inhibition experiments. Glycopeptides derived from horseradish peroxidase also failed to bind anticatalytic antibodies. Antibodies that inhibit enzyme activity have specificity for noncarbohydrate conformation dependent antigenic determinants of horseradish peroxidase. Additional experiments probed the mechanism by which inhibitory antibody decreases the catalytic activity of horseradish peroxidase. Absorption spectra of horseradish peroxidase that has bound Fab fragments sufficient to cause 90% inhibition of the enzyme activity determined that the enzyme retained the ability to bind hydrogen peroxide. Thus, anticatalytic antibodies do not prevent the formation of the first enzyme-substrate intermediate but mediate their inhibitory effects by disrupting a later step in the reaction mechanism.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
Conroy JM,Salter RDdoi
10.1016/0161-5890(82)90366-2subject
Has Abstractpub_date
1982-05-01 00:00:00pages
659-63issue
5eissn
0161-5890issn
1872-9142journal_volume
19pub_type
杂志文章abstract::Candida albicans the most frequently isolated clinical fungal pathogen can cause local as well as systemic and life-threatening infections particularly in immune-compromised individuals. A better and more detailed understanding how C. albicans evades human immune attack is therefore needed for identifying fungal immun...
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pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Molecular immunology
pub_type: 杂志文章
doi:10.1016/0161-5890(84)90069-5
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1016/j.molimm.2014.05.006
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pub_type: 杂志文章
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pub_type: 杂志文章
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pub_type: 杂志文章
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