Publication Date:
1986-05-23
Description:
A monoclonal antibody bound to a protein antigen decreases the rate of proteolytic cleavage of the antigen, having the greatest effect on those regions involved in antibody contact. Thus, an epitope can be identified by the ability of the antibody to protect one region of the antigen more than others from proteolysis. By means of this approach, two distinct epitopes, both conformationally well-ordered, were characterized on horse cytochrome c.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jemmerson, R -- Paterson, Y -- AI 19499/AI/NIAID NIH HHS/ -- AI21486/AI/NIAID NIH HHS/ -- GM 31841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 May 23;232(4753):1001-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2422757" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Antibodies, Monoclonal
;
*Antigen-Antibody Complex
;
Cytochrome c Group/*immunology
;
*Epitopes
;
Mice
;
Oligopeptides/immunology
;
Protein Conformation
;
Trypsin
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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