Abstract
Lactate dehydrogenase C, (LDH-C4) is an antigenic protein that occurs only in spermatozoa and the mature testis. The antibody-combining sites of this enzyme were mapped by measuring the binding of anti-LDH-C4 by isolated peptides. Pure mouse LDH-C4 was digested with trypsin, and the resulting fragments were fractionated by reverse-phase high-pressure liquid chromatography. Rabbit anti-mouse LDH-C4 bound to 13 pure peptides. Amino acid compositions and partial or complete sequencing by the Edman degradation was used to identify eight of these fragments in the complete structure of the molecule. The relationship between structure and antigenicity of these peptides is discussed in detail. These data fit best to the domain model of protein antigenicity. This antigenic map of LDH-C4 will be useful in the design of a synthetic contraceptive vaccine.
Original language | English (US) |
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Pages (from-to) | 643-649 |
Number of pages | 7 |
Journal | Molecular Immunology |
Volume | 22 |
Issue number | 6 |
DOIs | |
State | Published - Jun 1985 |
Funding
Acknowledgements-We thank Dr Joyce Shelton for critical reading of the manuscript. Excellent technical assistance was provided by Jean M. Severin and Eva Braun. This research was supported by grant HD05863 from the National Institutes of Health.
ASJC Scopus subject areas
- Molecular Biology
- Immunology