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Mouse Lactate Dchydrogenase (LDH) C 4 (Testis) Is Immunochemically Cross‐Reactive with LDH A 4 (Muscle) and LDH B 4 (Heart)
Author(s) -
WRIGHT L. L.,
SWOFFORD J. H.
Publication year - 1984
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1984.tb00926.x
Subject(s) - immunogen , antiserum , lactate dehydrogenase , cross reactivity , cross reactions , microbiology and biotechnology , biology , biochemistry , chemistry , enzyme , antigen , antibody , immunology , monoclonal antibody
It has been reported that lactale dehydrogenase (LDH) purified from testes (LDH C) of homotherms is not immunochemically cross‐reactive with somatic forms of LDH purified from heart (LDH B) or muscle (LDH A). On the basis of this premise, LDH C has been considered for use as a contraceptive vaccine. Data presented here indicate that mouse anlisera to either mouse or rat LDH C are cross‐reactive with LDH A and B purified from muscle and heart tissues of mice. However, rabbit antisera to mouse LDH C are not cross‐reactive with either mouse LDH A or B. Thus, the degree of cross‐reactivily is dependent on the species from which the immunogen LDH is purified, the antisera are derived, and the LDH used in the assay is purified. The determination that LDH A, B, and C are immunochemically cross‐reactive is of importance in evaluating LDH C as an immunogen in an immunologic approach to contraception.