Accession Number : ADA298707
Title : Antibody Specificity to Oncogene-Derived Peptides for Breast Cancer Detection.
Descriptive Note : Annual rept. 1 Jun 94-31 May 95,
Corporate Author : TORREY PINES INST FOR MOLECULAR STUDIES SAN DIEGO CA
Personal Author(s) : Pinilla, Clemencia ; Appel, Jon R.
PDF Url : ADA298707
Report Date : 01 JUL 1995
Pagination or Media Count : 19
Abstract : This report describes the initial work carried out on the specifcity of two peptide-antibody interactions. Monoclonal antibody 172-12A4, which was raised against the peptide LGSGAFGTIYKGC from V-erbB, was screened against several peptide libraries and yielded individual sequences that were recognized with high affinities. Also, a complete set of individual substitution analogs for each position of the antigenic determinant of this peptide was synthesized. This set of analogs was assayed by direct and competitive ELISA to determine the replaceability and relative positional importance of each residue. Four out of eight residues were found to be highly specific in which no substitution was permitted. In the second example, mAb 121-15B10, which was raised against lGRGNFGEVFSGC from v-fes, was screened against peptide libraries yielding a profile of specific and redundant residues. The understanding of the specificities of these antibodies at the amino acid level will help in the development of these antibodies as early diagnostics in breast cancer.
Descriptors : *DETECTION, *PEPTIDES, *AMINO ACIDS, *CANCER, *MAMMARY GLANDS, COMPETITION, ENZYMES, DIAGNOSIS(GENERAL), ANTIBODIES, ANALOGS, SUBSTITUTES, IMMUNOASSAY, REDUNDANCY, LIBRARIES, RESIDUES.
Subject Categories : Anatomy and Physiology
Medicine and Medical Research
Distribution Statement : APPROVED FOR PUBLIC RELEASE