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Mitochondrial DNA sequence relationships of the extinct blue antelope Hippotragus leucophaeus

Mitochondrial DNA sequence relationships of the extinct blue antelope Hippotragus leucophaeus crystallin (60 to 110 mU per mg to total protein [11]). These latter values are due to normal, anaerobic glycolysis in the lens. The high values in Phelsuma indicate that e-crystallin is expressed as an active enzyme, similar to the situation in birds. It has been proposed that the recruitment as crystallins of NAD(P)H-binding enzymes, which causes increased levels of reduced pyridine nucleotides, could protect the lens against oxidative stress and/or serve to reduce glare at wavelengths in the near UV [4, 7, 12]. eCrystallin has - with the exception of the nocturnal caiman - indeed been found only in lenses of diurnal species. However, the possession of e-crystallin or other NAD(P)H-binding enzyme crystallins cannot be a decisive requirement for effective functioning of lenses in diurnal animals, as there are many diurnal birds and reptiles without such crystallins, e.g., the fully diurnal geckonid genera Lygodactylus and Gonatodes [13]. It may be noted that the Phelsuma lens is remarkable for the complexity of its composition: it contains, in addition to the ubiquitous a-, fl-, and y-crystallins, no less than four enzyme crystallins: 6/argininosuccinate lyase, r/ct-enolase, ~z/glyceraldehyde 3-phosphate dehydrogenase, and e / L D H [4, 11] (Fig. 1). The http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Naturwissenschaften Springer Journals

Mitochondrial DNA sequence relationships of the extinct blue antelope Hippotragus leucophaeus

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References (13)

Publisher
Springer Journals
Copyright
Copyright © 1996 by Springer-Verlag
Subject
Life Sciences; Life Sciences, general; Environment, general
ISSN
0028-1042
eISSN
1432-1904
DOI
10.1007/BF01143060
Publisher site
See Article on Publisher Site

Abstract

crystallin (60 to 110 mU per mg to total protein [11]). These latter values are due to normal, anaerobic glycolysis in the lens. The high values in Phelsuma indicate that e-crystallin is expressed as an active enzyme, similar to the situation in birds. It has been proposed that the recruitment as crystallins of NAD(P)H-binding enzymes, which causes increased levels of reduced pyridine nucleotides, could protect the lens against oxidative stress and/or serve to reduce glare at wavelengths in the near UV [4, 7, 12]. eCrystallin has - with the exception of the nocturnal caiman - indeed been found only in lenses of diurnal species. However, the possession of e-crystallin or other NAD(P)H-binding enzyme crystallins cannot be a decisive requirement for effective functioning of lenses in diurnal animals, as there are many diurnal birds and reptiles without such crystallins, e.g., the fully diurnal geckonid genera Lygodactylus and Gonatodes [13]. It may be noted that the Phelsuma lens is remarkable for the complexity of its composition: it contains, in addition to the ubiquitous a-, fl-, and y-crystallins, no less than four enzyme crystallins: 6/argininosuccinate lyase, r/ct-enolase, ~z/glyceraldehyde 3-phosphate dehydrogenase, and e / L D H [4, 11] (Fig. 1). The

Journal

Naturwissenschaften – Springer Journals

Published: Apr 1, 1996

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