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Cloning, sequencing, and characterization of LDH‐C 4 from a fox testis cDNA library
Author(s) -
Bradley Mark P.,
Geelan Amber,
Leitch Virginia,
Goldberg Erwin
Publication year - 1996
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/(sici)1098-2795(199608)44:4<452::aid-mrd4>3.0.co;2-k
Subject(s) - biology , complementary dna , cdna library , microbiology and biotechnology , peptide sequence , cloning (programming) , sperm , blot , epitope , lactate dehydrogenase , protein subunit , sequence analysis , messenger rna , antibody , gene , genetics , biochemistry , enzyme , computer science , programming language
A full‐length cDNA encoding the sperm‐specific enzyme lactate dehydrogenase‐C 4 was isolated from a fox testis cDNA expression library and sequenced. The deduced translated protein sequence was shown to be 86% identical to that of human LDH‐C 4 . In the fox testis, mRNA encoding LDH‐C 4 was first detected in pachytene spermatocytes. The LDH‐C 4 protein monomer was identified in Western blots of sperm membrane extracts as having a molecular weight of approximately 35,000, consistent with the monomeric size of this subunit previously identified in sperm from other species. The LDH‐C 4 protein is localized on the sperm plasma membrane overlying the principal piece of the tail. Based on the available sequence data, we were able to identify an epitope within the N‐terminal region of the LDH‐C 4 amino‐acid sequence which when administered to female foxes is antigenic and produces antibodies capable of recognizing the native protein. © 1996 Wiley‐Liss, Inc.