scholarly journals Partial purification and properties of Halobacterium cutirubruml-alanine dehydrogenase

1977 ◽  
Vol 161 (2) ◽  
pp. 313-320 ◽  
Author(s):  
E K Kim ◽  
P S Fitt
Keyword(s):  
Reductive Amination ◽  
Partial Purification ◽  
Oxidative Deamination ◽  
Alanine Dehydrogenase ◽  
Amination Reaction ◽  
Absolute Requirement ◽  
Purification And Properties ◽  
High Concentrations

1. Halobacterium cutirubrum L-alanine dehydrogenase was purified approx. 100-fold. 2. It has a mol. wt. of 72 500, about one-third that of two well-studied alanine dehydrogenases from non-halophiles. 3. The activity of the enzyme increases with temperature up to 70 degrees C, but the protein itself is not thermostable. 4. In the reductive amination reaction, the enzyme is fully active in the presence of high concentrations of K+, Na+ or NH4+ and partially active with Cs+ or Li+, but for oxidative deamination it has an absolute requirement for K+.

scholarly journals Einfluß von Effektoren auf Molekulargewicht und Aktivität von Glutamat-Dehydrogenase (GluDH) aus Rinderleber in vitro / The Influence of Various Effectors on Molecular Weight and Activity of Bovine Liver

1970 ◽  
Vol 25 (6) ◽  
pp. 587-589
Author(s):  
M. Kempfle ◽  
K.-O. Mosebach ◽  
C. Blanke
Keyword(s):  
Molecular Weight ◽  
Glutamic Acid ◽  
Active Sites ◽  
Reductive Amination ◽  
Bovine Liver ◽  
Oxidative Deamination ◽  
Acid Reaction ◽  
High Concentrations ◽  
Enzyme Molecules

The activities of GluDH against glutamic acid (α-oxoglutarate) and against alanine (pyruvate) were compared unter various conditions. Diethylstilbestrole (DES) inhibited the oxidative deamination of glutamic acid at all enzyme concentrations investigated but its effect on the oxidative deamination of alanine was different. At small enzyme concentrations (<0.01 mg/ml) where there are only monomers of the enzyme (mol.-weight 310 000) DES inhibited analogously to its behaviour in the glutamic acid reaction. At high concentrations where almost only aggregated enzyme molecules are present, DES stimulated the deamination of alanine and the reductive amination of pyruvate, respectively. These observations are interpreted without assuming different conformations of the monomers obtained either by simple dilution or by treatment with DES. An interpretation is possible by conceiving the inhibition and liberation of the active sites to be events influencing the encymatic activity contrarily.

scholarly journals Partial purification and properties of l-asparagine synthetase from mouse pancreas

1979 ◽  
Vol 181 (1) ◽  
pp. 51-59 ◽  
Author(s):  
Harry A. Milman ◽  
David A. Cooney
Keyword(s):  
Specific Activity ◽  
Asparagine Synthetase ◽  
Partial Purification ◽  
Synthetase Activity ◽  
Mouse Pancreas ◽  
Purification And Properties ◽  
Bean Trypsin Inhibitor ◽  
Thiol Reagent ◽  
High Concentrations ◽  
Glutaminase Activity

l-Asparagine synthetase was partially purified from mouse pancreas to a final mean specific activity of 0.10 unit/mg of protein. The enzyme exhibited an l-glutaminase activity which was not affected by l-asparate, NH4Cl, ATP–MgCl2, l-glutamate, AMP (sodium salt) or sodium pyrophosphate. The l-glutamine-dependent l-asparagine synthetase activity of the partially purified enzyme from mouse pancreas was markedly decreased by freezing for 7 days at −87°C in the presence of 1mm-dithiothreitol, but effectively protected from inactivation by high concentrations (10mm) of the thiol reagent. The l-glutaminase activity of the enzyme was inhibited by antagonists of l-glutamine (e.g. 6-diazo-5-oxo-l-norleucine, 5-chloro-4-oxo-l-norvaline, 5-diazo-4-oxo-l-norvaline and NSC-163501) and thiol-reactive compounds (e.g. 2-amino-4-arsenophenol hydrochloride, maleimide, mucochloric acid and ZnCl2), but not by aminomalonic acid, the next lower homologue of l-aspartate, nor by l-homoserine β-adenylate, an analogue of the presumed transitory covalent intermediate. The complete forward reaction catalysed by l-asparagine synthetase from mouse pancreas appears to be irreversible and essentially stoicheiometric under the conditions examined. Mouse pancreas contains a proteolytic inhibitor of l-asparagine synthetase separable from the enzyme by ion-exchange column chromatography. The inhibitor is activated by incubation at 4°C for 110h and inactivated by soya-bean trypsin inhibitor, di-isopropyl phosphorofluoridate and boiling.

Partial purification and properties of an endo-xylanase from cucumber seeds

1991 ◽  
Vol 81 (3) ◽  
pp. 327-334 ◽  
Author(s):  
Cesar V. Mujer ◽  
Dale W. Kretchman ◽  
A. Raymond Miller
Keyword(s):  
Partial Purification ◽  
Purification And Properties

Partial purification and properties of a 36-kDa 1-aminocyclopropane-l-carboxylate N-malonyltransferase from mung bean

1995 ◽  
Vol 94 (4) ◽  
pp. 629-634 ◽  
Author(s):  
Mohamed Benichou ◽  
Gracia Martinez-Reina ◽  
Felix Romojaro ◽  
Jean-Claude Pech ◽  
Alain Latche
Keyword(s):  
Mung Bean ◽  
Partial Purification ◽  
Purification And Properties

scholarly journals Partial purification and properties of a pre-mRNA splicing activity.

1985 ◽  
Vol 260 (2) ◽  
pp. 1096-1102
Author(s):  
P R DiMaria ◽  
G Kaltwasser ◽  
C J Goldenberg
Keyword(s):  
Mrna Splicing ◽  
Partial Purification ◽  
Purification And Properties

Partial Purification and Properties of Human Brain Aldehyde Dehydrogenases

1985 ◽  
Vol 45 (6) ◽  
pp. 1903-1910 ◽  
Author(s):  
Jacques-Andre Maring ◽  
Richard A. Deitrich ◽  
Roger Little
Keyword(s):  
Human Brain ◽  
Partial Purification ◽  
Aldehyde Dehydrogenases ◽  
Purification And Properties
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