Nom du corpus

Corpus Systématique Animale

Titre du document

Kinetic comparison of caiman ?-crystallin and authentic lactate dehydrogenases of vertebrates

Lien vers le document
Éditeur
Springer (journals)
Langue(s) du document
Anglais
Type de document
Research-article
Mots-clés d'auteur
  • Lens crystallin
  • ?-crystallin
  • lactate dehydrogenase
  • enzyme kinetics
  • isozyme electrophoresis
  • eye lens
  • duck
  • caiman
Nom du fichier dans la ressource
Oiseaux_v2b_02315, Reptiles_v2b_00721
Auteur(s)
  • Shyh-Horng Chiou 1
  • Hwei-Jen Lee 2
  • Shih-Ming Huang 2
  • Gu-Gang Chang 2
Affiliation(s)
  • 1) Laboratory of Crystallin Research, Institute of Biochemical Sciences, National Taiwan University and Institute of Biological Chemistry, Academia Sinica, P.O. Box 23-106, Taipei, Taiwan 10098, Republic of China
  • 2) Department of Biochemistry, National Defense Medical Center, Taipei, Taiwan 10764, Republic of China
Résumé

Kinetic comparison of ?-crystallins isolated from the avian and reptilian species and the authentic lactate dehydrogenases (LDHs) was undertaken in order to clarify the identities of these structural lens proteins in relation to their enzymatic activity. Caiman ?-crystallin similar to the previously characterized duck ?-crystallin appeared to possess a genuine and stable LDH activity as detected by nitro blue tetrazolium staining on polyacrylamide gels and conventional kinetic assays. Kinetic parameters for pyruvate,l-lactate, NAD+, and three structural analogues of the coenzyme in this ?-crystallin catalyzed reaction were also determined and compared. Despite the structural similarities between ?-crystallins and chicken heart LDH, differences in charge and kinetic properties have been revealed by native isozyme electrophoresis and kinetic analysis as examined by initial velocity and substrate inhibition studies. It is found that the kinetic data analyzed for caiman ?-crystallin were more fitted with a compulsory ordered Bi-Bi sequential mechanism similar to those for the authentic LDHs and duck ?-crystallin. Caiman ?-crystallin has for the first time been established as a heart-type LDH based on the kinetic analysis and comparison with the authentic heart- and muscle-type LDHs from pig and chicken.

Catégories Science-Metrix
  • 1 - health sciences
  • 2 - biomedical research
  • 3 - biophysics
Catégories INIST
  • 1 - sciences appliquees, technologies et medecines
  • 2 - sciences biologiques et medicales
  • 3 - sciences biologiques fondamentales et appliquees. psychologie
  • 4 - psychologie. psychophysiologie
Catégories Scopus
  • 1 - Life Sciences ; 2 - Biochemistry, Genetics and Molecular Biology ; 3 - Biochemistry
Identifiant ISTEX
1439E5D1F68862EF3930DB06DDAE5E90BD03236B
Revue

Journal of Protein Chemistry

Année de publication
1991
Présence de XML structuré
Non
Version PDF
1.3
Score qualité du texte
7.111
Sous-corpus
  • Oiseaux
  • Reptiles
Type de publication
Journal
ark:/67375/1BB-724F83G6-F
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