Characterization and comparison of epsilon-crystallin and lactate dehydrogenases in the lenses of vertebrates and invertebrates
Chiou, S.H.; Chang, W.P.; Chen, C.C.
Biochemistry International 18(6): 1093-1100
1989
ISSN/ISBN: 0158-5231 PMID: 2787637 Document Number: 339961
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.