The mechanism of triosephosphate dehydrogenase inactivation by reduced diphosphopyridine nucleotide.

نویسندگان

  • R AMELUNXEN
  • S GRISOLIA
چکیده

We have shown in a previous communication (1) that the enzyme triosephosphate dehydrogenase is rapidly inactivated in the presence of reduced diphosphopyridine nucleotide at physiological concentrations, temperature, and pH. Good stoichiometry was shown for the amount of enzyme inactivation, DPNH-X1 formation, and disappearance of sulfhydryl groups. It was then of particular interest to determine the detailed mechanism of the inactivation phenomenon and whether or not these indicated changes were truly related. As shown in this paper, the mechanism of DPNH-induced enzyme inactivation has been clarified, and DPNH-X formation and enzyme inactivation can be differentiated.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Automated assay of activities of enzymes involving the diphosphopyridine nucleotide-reduced diphosphopyridine nucleotide reaction.

A continuous flow instrumental system of analysis, first described by Skeggs (l), was previously applied to the determination of phosphohexose isomerase activity and resulted in a method that was approximately eightfold as rapid as the manual procedure (2). The present paper is concerned with the application of this system of analysis to the determination of enzyme activities that utilize the d...

متن کامل

Kinetic Studies of Dogfish Liver Glutamate Dehydrogenase with Diphosphopyridine Nucleotide and the Effect of Added Salts*

Kinetic studies have been performed with crystalline dogfish liver glutamate dehydrogenase with the diphosphopyridine nucleotides as cofactors. The kinetic constants for the various substrates have been determined. In its sensitivity to guanosine S-triphosphate, adenosine S&phosphate, and excess reduced diphosphopyridine nucleotide the enzyme is similar to that derived from other vertebrates. T...

متن کامل

The reaction of methyl mercury nitrate with the sulfhydryl groups of yeast glyceraldehyde-3-phosphate dehydrogenase.

The importance of two of the thiol groups of yeast triosephosphate dehydrogenase for its activity haa been shown by the abolition of activity and diphosphopyridine nucleotide binding by the addition of 2 equivalents of p-chloromercuribenzoate (PCMB) (1, 2). The reaction of methyl mercury nitrate with this enzyme has been found to be anomalous in the sense that this mercury compound, unlike PCMB...

متن کامل

Kinetic studies of dogfish liver glutamate dehydrogenase with diphosphopyridine nucleotide and the effect of added salts.

Kinetic studies have been performed with crystalline dogfish liver glutamate dehydrogenase with the diphosphopyridine nucleotides as cofactors. The kinetic constants for the various substrates have been determined. In its sensitivity to guanosine S-triphosphate, adenosine S&phosphate, and excess reduced diphosphopyridine nucleotide the enzyme is similar to that derived from other vertebrates. T...

متن کامل

Stereospecificity of hydrogen transfer by pyridine nucleotide-linked hydroxysteroid dehydrogenases.

The present studies are concerned with the determination of the steric course of the transfer of hydrogen catalyzed by hydroxysteroid dehydrogenases. The classic work of Vennesland et al. (l-3) has demonstrated that pyridine nucleotide-linked dehydrogenases catalyze a direct and stereospecific transfer of hydrogen between the substrate and the para position of the nicotinamide ring of the nucle...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 237  شماره 

صفحات  -

تاریخ انتشار 1962