Octopine Dehydrogenase
- 1 July 1972
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 28 (2) , 261-268
- https://doi.org/10.1111/j.1432-1033.1972.tb01909.x
Abstract
The amino acid composition of octopine dehydrogenase from muscles of Pecten maximus was determined. The calculate dpartial specific volume of 0.74 allowed us to evaluate the molecular weight of the enzyme as 38000.It is concluded that this enzyme consists of a single polypeptide chain on the basis of the molecular weight determined from equilibrium ultracentrifugation in 6 M guanidine hydrochloride and from electrophoresis on polyacrylamide gel containing sodium dodecylsulfate as well as on the basis of the number of peptides obtained by tryptic digestion. The presence of one essential –SH group per mole of enzyme and of one binding site for NADH are also consistent with the existence of a single active center.No NH2‐terminal amino acid can be detected by reaction with dansyl chloride and with phenyl‐isothiocyanate.This publication has 51 references indexed in Scilit:
- Comparative Structural Studies of the Active Site of ATP‐Guanidine PhosphotransferasesEuropean Journal of Biochemistry, 1969
- Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenasesBiochemistry, 1969
- Amino-acid Sequence of Glyceraldehyde 3-Phosphate Dehydrogenase from Lobster MuscleNature, 1967
- Isopiestic compositions as a measure of preferential interactions of macromolecules in two-component solvents. Application to proteins in concentrated aqueous cesium chloride and guanidine hydrochlorideJournal of the American Chemical Society, 1967
- The subunits of bovine liver glutamate dehydrogenase: Demonstration of a single peptide chainJournal of Molecular Biology, 1966
- The involvement of a tryptophan residue of glutamate dehydrogenase in the binding of L-glutamateBiochemical and Biophysical Research Communications, 1965
- The DPNH-binding capacity of various dehydrogenasesBiochemical and Biophysical Research Communications, 1964
- Measurement of protein-binding phenomena by gel filtrationBiochimica et Biophysica Acta, 1962
- Eine Mikrobestimmung von Amid-Stickstoff, speziell in ProteinenHoppe-Seyler´s Zeitschrift Für Physiologische Chemie, 1958
- Spectrophotometric Study of the Reaction of Protein Sulfhydryl Groups with Organic MercurialsJournal of the American Chemical Society, 1954