TY - JOUR
T1 - Characterization of monoclonal antibodies to the sperm-specific lactate dehydrogenase isozyme.
AU - Goldman-Leikin, R. E.
AU - Goldberg, E.
PY - 1983/6
Y1 - 1983/6
N2 - The isozyme of lactate dehydrogenase (LDH) that is specific to testes, designated LDH-C4, is the predominant LDH isozyme in mammalian spermatozoa. Four high-affinity monoclonal antibodies have been developed to murine LDH-C4. These antibodies were tested for crossreactivity with LDH-C4 from rat, hamster, rabbit, and human by competitive binding radioimmunoassays. Monoclonal antibodies RG-1 and RG-2 are specific for adjacent or partially overlapping epitopes. The other two monoclonal antibodies each recognize separate and distinct determinants. One of these, designated RG-4, recognizes a sequential determinant that is contained in the coenzyme binding loop, residues 101-115 of the C subunit. Furthermore, RG-4 shows reduced binding affinity for rat LDH-C4 which differs in amino acid sequence at residue 108 and 111 in this region of the molecule. RG-4 also has reduced affinity for LDH-C4 of other species, which is consistent with substitutions in the amino acid sequences of the coenzyme binding loop. These differences between C4 of closely related species is in contrast to the high degree of conservation of this sequence in the LDH-A4 and LDH-B4 isozymes. These results provide useful information regarding homologies among species of LDH-C4 as well as the evolution of this isozyme.
AB - The isozyme of lactate dehydrogenase (LDH) that is specific to testes, designated LDH-C4, is the predominant LDH isozyme in mammalian spermatozoa. Four high-affinity monoclonal antibodies have been developed to murine LDH-C4. These antibodies were tested for crossreactivity with LDH-C4 from rat, hamster, rabbit, and human by competitive binding radioimmunoassays. Monoclonal antibodies RG-1 and RG-2 are specific for adjacent or partially overlapping epitopes. The other two monoclonal antibodies each recognize separate and distinct determinants. One of these, designated RG-4, recognizes a sequential determinant that is contained in the coenzyme binding loop, residues 101-115 of the C subunit. Furthermore, RG-4 shows reduced binding affinity for rat LDH-C4 which differs in amino acid sequence at residue 108 and 111 in this region of the molecule. RG-4 also has reduced affinity for LDH-C4 of other species, which is consistent with substitutions in the amino acid sequences of the coenzyme binding loop. These differences between C4 of closely related species is in contrast to the high degree of conservation of this sequence in the LDH-A4 and LDH-B4 isozymes. These results provide useful information regarding homologies among species of LDH-C4 as well as the evolution of this isozyme.
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U2 - 10.1073/pnas.80.12.3774
DO - 10.1073/pnas.80.12.3774
M3 - Article
C2 - 6574516
AN - SCOPUS:0020773535
SN - 0027-8424
VL - 80
SP - 3774
EP - 3778
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 12
ER -