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KMID : 0578319940040020225
Molecules and Cells
1994 Volume.4 No. 2 p.225 ~ p.230
Characterization of Immunologically Distinct Pyruvate Dehydrogenase E1¥á Subunit Present in Rat Testis
Huh, Tae-Lin
Ryu, jae-Ha/Huh, Jse-Wook/Casazza, Joseph P./Veech, Richard L./Song, Byoung J.
Abstract
The tissue distribution of the pyruvate dehydrogenase complex (PDC) in several rat tissues was examined. Different amounts of immunoreactive proteins of pyruvate dehydrogenase (PDH) Ela Elp, E2, and E3 subunits were observed in five rat tissues with a decreasing order of PDC activities in heart > kidney > brain > liver -> testis. Most subunits of the PDC appeared to he normal in size and immunoreactivities toward their corresponding polyclonal antibodies. However, virtually no immunoreactive PDH Ela subunit (Mr 41,000) was detected in testis while it was readily detected in other tissues examined, suggesting that the PDH Ela subunit present in rat testis may represent an immunologically distinct isoform. The testis-specific PDH Ela isoform was confirmed by immunoblot analysis using polyclonal antibodies against a synthetic peptide with the amino acid sequence around two major phosphorylation sites of PDH Ela subunit. Unlike the regular PDH Ela subunit (Mr 41,000) in the heart and kidney, the apparent molecular mass of PDH Ela isoform in testis of all four rat strains examined appeared to be 56,000 Da on SDS-polyacrylamide gel electrophoresis, representing a new class of PDH Ela subunit.
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