Characterization and comparison of epsilon-crystallin and lactate dehydrogenases in the lenses of vertebrates and invertebrates.
Screening of lens homogenates for the identification of lactate dehydrogenases was undertaken for the representative species from five major classes of vertebrates plus the cephalopod of invertebrates. The duck and caiman lenses appeared to contain the highest enzymatic activity of this glycolytic enzyme among all species examined. Biochemical isolation and characterization of epsilon-crystallins from the duck and caiman lenses revealed differences between these structural crystallins and the authentic lactate dehydrogenase of the avian heart regarding some of the kinetic properties. This is in contrast with the claim that duck epsilon-crystallin is identical to heart-type lactate dehydrogenase.
Chiou
S H
SH
Institute of Biochemical Sciences, National Taiwan University, R.O.C.
Chang
W P
WP
Chen
C C
CC
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001188:Artiodactyla; D002347:Carps / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D003459:Crystallins / Q000032:analysis* / Q000378:metabolism; D049832:Decapodiformes / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007448:Invertebrates / Q000378:metabolism*; D007770:L-Lactate Dehydrogenase / Q000032:analysis* / Q000378:metabolism; D007908:Lens, Crystalline / Q000032:analysis* / Q000201:enzymology; D011200:Poultry / Q000378:metabolism; D011892:Rana catesbeiana / Q000378:metabolism; D012104:Reptiles / Q000378:metabolism; D013053:Spectrophotometry; D014714:Vertebrates / Q000378:metabolism*
D000596:Amino Acids; D003459:Crystallins; D007770:L-Lactate Dehydrogenase