The Content and Action of Diphosphopyridine Nucleotide in Triosephosphate Dehydrogenase

Murdock, Archie L.; Koeppe, Owen J.

doi:10.1016/s0021-9258(18)91294-9

Cited by 86 publications

(24 citation statements)

References 25 publications

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“…The spectrum of the glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle and B. coagulans (grown at either 37 or 55 °C) exhibits an absorbance maximum around 275-276 nm which yields an extinction coefficient of 1.03 ± 0.04 and 0.80 ± 0.06 cm2 mg-1, respectively. The value for the rabbit muscle enzyme is con-sistent with the previously reported Ene of 1.06 (Murdock and Koeppe, 1964), whereas the lower value for the enzyme from B. coagulans can be attributed to the decreased tryptophan content as shown below for the calculated extinction coefficient at 280 nm. The Ano'.Aieo ratio of 1.28 for the enzyme from B. coagulans grown at 37 and 55 °C clearly indicates that the enzyme contains firmly bound NAD+.…”

Section: Resultssupporting

confidence: 85%

Purification and characterization of thermolabile glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans KU

1977

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Section: Resultssupporting

confidence: 85%

Purification and characterization of thermolabile glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans KU

1977

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“…1968;Jaenicke et al, 1968). ApoGPDH was prepared essentially by the method of Murdock and Koeppe (1964) except that the ratio of charcoal pulp to protein was doubled and the EDTA solution was adjusted to pH 8 with NaOH.…”

Section: Methodsmentioning

confidence: 99%

Effect of heavy water and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase

Smith¹,

Schachman²

1973

Biochemistry

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The binding of successive nicotinamide adenine dinucleotide (NAD) molecules to the subunits of rabbit muscle glyceraldehyde phosphate dehydrogenase was found by the technique of difference sedimentation to cause an inherent change in the sedimentation coefficient of the protein beyond that attributable to the buoyant weight of the coenzyme. Attempts were made to determine whether the measured changes in sedimentation coefficient were wholly or partially due to shifts in the association-dissociation equilibria between the enzyme and its subunits. The results were equivocal because aqueous preparations of the apoenzyme, produced by charcoal treatment, showed with time increasing amounts of subunits and aggregates larger than tetramers.This spontaneous conversion was accompanied by the loss of potential enzymic activity. Marked stabilization of the apoenzyme was achieved through the use of buffered D20 solutions. The spontaneous inactivation and precipitation observed in aqueous solutions were strikingly eliminated in D20 solutions even at room temperature. In addition, for most preparations of the enzyme in the absence or presence of NAD only tetramers could be detected by sedimentation equilibrium measurements over the concentration range from 0.1 to 3.0 g per 1. This finding was confirmed by differential sedimentation studies which provided direct measurements of the concentration dependence of the sedimentation coefficient. For those preparations showing no evident dissociation in the sedimentation equilibrium experiments the differential sedimentation technique gave similar results for the apoenzyme and enzyme to which different amounts T> X V_abbit muscle glyceraldehyde phosphate dehydrogenase,1 though consisting apparently of four identical polyt From the

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“…The results obtained for native proteins were in agreement with those obtained by other workers. 2,4,5,10,[17][18][19][20][21][22] [ 203 Hg]PHMB reacts with a larger number of -SH groups in denatured proteins than native proteins. This result is expected considering that denaturation would unfold the protein, thus exposing buried -SH groups.…”

Section: Resultsmentioning

confidence: 99%

“…Table 4 summarises the values reported in the literature obtained by using other procedures. 2,4,5,10,[17][18][19][20][21][22] A comparison of the results obtained by different methods is of interest and shows a good agreement. However, because of the different reactivities of -SH groups, 'no single analytical procedure based on one or the other reaction of -SH groups with "-SH reagents" can actually be regarded as conclusive by itself'.…”

Section: Resultsmentioning

confidence: 99%

203Hg labelled PHMB as reagent for the determination of –SH groups in native and denatured proteins by hydrophobic interaction chromatography

Raspi¹,

Bramanti²,

Spinetti³

et al. 1999

Analyst

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Aldolase, glyceraldehyde 3-phosphate dehydrogenase and ovalbumin were determined by hydrophobic interaction chromatography, which allows the evaluation of the number of -SH groups per molecule of protein in both the native and denatured form. These proteins were chosen as models to show the generality of use of the procedure for analytical and biochemical applications. The experiments were performed by using 203 Hg-labelled p-hydroxymercuribenzoate as reagent and known concentrations of proteins. The results were compared with FI-CV-ETAAS measurements and literature data.

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The Content and Action of Diphosphopyridine Nucleotide in Triosephosphate Dehydrogenase

Cited by 86 publications

References 25 publications

Purification and characterization of thermolabile glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans KU

Purification and characterization of thermolabile glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans KU

Effect of heavy water and nicotinamide adenine dinucleotide on the sedimentation properties and structure of glyceraldehyde phosphate dehydrogenase

203Hg labelled PHMB as reagent for the determination of –SH groups in native and denatured proteins by hydrophobic interaction chromatography

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