Abstract
A tentative amino acid sequence of mouse testicular lactate dehydrogenase C4 was deduced from an electron density map and comparison with five other known lactate dehydrogenase sequences. The amino acid composition determined by chemical analysis agrees reasonably well with the present results. Necessary changes in amino acids were largely conservative and confined to the external portions of the molecule. Residues in the Q and P subunit contact regions were particularly well conserved as were most internal residues. The minimum base change/codon was similar between the C and H isoenzymes and between the C and M isoenzymes.
Highlights
A tentative amino acid sequence of mouse testicular lactate dehydrogenase C4 was deduced from an electron density map and comparison with five other known lactate dehydrogenase sequences
The H- and M-type LDHs are characteristic of heart and muscle tissues, respectively [2]. In addition to these somatic isoenzymes, a third form, LDH C, is found uniquely in spermatogenic tissue. While synthesis of both H and M polypeptides may occur in the sperm cell, C subunit synthesis begins after H and M subunit production ceases [3]
This results in the physiological isolation of C subunits from the H and M types so that only C tetramers are generated in viva [4]
Summary
A tentative amino acid sequence of mouse testicular lactate dehydrogenase C4 was deduced from an electron density map and comparison with five other known lactate dehydrogenase sequences. Residues in the Q and P subunit contact regions were well conserved as were most internal residues. Pending the availability of direct chemical information, a tentative amino acid sequence for the C isoenzyme was deduced from an inspection of the electron density map taking into account the five known LDH sequences [7,8,9].
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