Crystalline Aldolase

Taylor, John Fuller; Green, Arda Alden; Cori, Gerty T.

doi:10.1016/s0021-9258(18)57431-7

Cited by 291 publications

(17 citation statements)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The predictions of diffusion coefficients based on the molecular weights were made according to the Young–Carroad–Bell model in aqueous solution at 20 °C (ref ). The diffusion coefficients of enzymes from FCS measurements (solid circles) can be found in Table ; the reported diffusion coefficients from other methods (open circles) are hexokinase, 56.4 μm 2 /s, ref ; aldolase, 46.3 μm 2 /s, ref ; catalase, 41 μm 2 /s, ref ; F 1 -ATPase, 31 μm 2 /s, ref ; and urease, 31 μm 2 /s, ref .…”

Section: Experimental Observationsmentioning

confidence: 99%

Enhanced Diffusion of Catalytically Active Enzymes

Zhang

Hess

2019

ACS Cent. Sci.

View full text Add to dashboard Cite

The past decade has seen an increasing number of investigations into enhanced diffusion of catalytically active enzymes. These studies suggested that enzymes are actively propelled as they catalyze reactions or bind with ligands (e.g., substrates or inhibitors). In this Outlook, we chronologically summarize and discuss the experimental observations and theoretical interpretations and emphasize the potential contradictions in these efforts. We point out that the existing multimeric forms of enzymes or isozymes may cause artifacts in measurements and that the conformational changes upon substrate binding are usually not sufficient to give rise to a diffusion enhancement greater than 30%. Therefore, more rigorous experiments and a more comprehensive theory are urgently needed to quantitatively validate and describe the enhanced enzyme diffusion.

show abstract

Section: Experimental Observationsmentioning

confidence: 99%

Enhanced Diffusion of Catalytically Active Enzymes

Zhang

Hess

2019

ACS Cent. Sci.

View full text Add to dashboard Cite

show abstract

“…The preparation of RAMA 10 The ground skeletal muscle of a rabbit was extracted in a cold room at 5 ЊC with two equal portions of cold water (or cold 0.03 M NaOH, or KOH) and strained through gauze. The cold extract (1200 ml) was first brought to pH 7.5 with dil.…”

Section: Methodsmentioning

confidence: 99%

Synthesis of perfluoroalkylated sugars catalyzed by rabbit muscle aldolase (RAMA)

Zhu

2000

J. Chem. Soc., Perkin Trans. 1

View full text Add to dashboard Cite

“…1 In yeast and most animal cells fructose diphosphate is split into two triose phosphate moieties by aldolase; one of these, phosphoglyceraldehyde, is oxidized by its dehydrogenase (Warburg's oxidizing enzyme) with concomitant reduction of DPN (see reference 19). The test as here employed measures the rate of the slower of these two enzymatic reactions in the egg extracts.…”

Section: Datementioning

confidence: 99%

Glucose-6-Phosphate and 6-Phosphogluconate Dehydrogenases From Eggs of the Sea Urchin, Arbacia Punctulata

Krahl

Keltch

Walters

et al. 1955

The Journal of General Physiology

View full text Add to dashboard Cite

Glucose-6-phosphate dehydrogenase (Zwischerfferment) and 6-phosphogluconate dehydrogenase, first studied in y e a s t by Warburg and his coworkers (1, 2), have since been found in a number of cells and tissues. These have received extensive study because they provide a pathway for formation of pentose phosphate from hexose phosphate and because of the possibility that oxidation of glucose-6-phosphate by this means may provide energy for function. (See references 3--6.)The present experiments deal with the occurrence, the properties, and the relation to over-all metabolism of these two enzymes in eggs of the sea urchin, Arbacia punctulata; they are part of a general survey of the enzymes of Arbacia eggs (7). Experimental MethodsThe eggs were obtained and handled as previously described (8, 9). Homogenates were prepared as before (9), except that citrate was omitted from, and 0.004 ~ ethylenediamine tetraacetic acid included in, the homogenizing medium to minimize breakdown of the echinochrome granules; the homogenates were a light orange-pink and the supernatant fractions obtained therefrom by centrifugation at 20,000 g for 30 minutes were clear and of a straw yellow color. The homogenates and other fractions to be tested were kept at ice water temperature; full activity was retained for 6 to 8 hours; 20 to 40 per cent of the initial activity of the homogenate or supematant fractions was lost by a single freezing and thawing; this procedure appeared relatively more damaging to the phosphogluconate dehydrogenase than to glucose-6-phosphate dehydrogenase. The values recorded in the tables and figures were calculated by use of the conversion factors previously derived (10).The sources of the special reagents were: Sigma Chemical Company, triphosphopyridine nucleotide (TPN), 83 per cent purity (assayed by yeast Zwischenferment), barium glucose-l-phosphate, and yeast Zwischenferment (lot No. 54-137, virtually free of phosphogluconate dehydrogenase);

show abstract

Crystalline Aldolase

Cited by 291 publications

References 15 publications

Enhanced Diffusion of Catalytically Active Enzymes

Enhanced Diffusion of Catalytically Active Enzymes

Synthesis of perfluoroalkylated sugars catalyzed by rabbit muscle aldolase (RAMA)

Glucose-6-Phosphate and 6-Phosphogluconate Dehydrogenases From Eggs of the Sea Urchin, Arbacia Punctulata

Contact Info

Product

Resources

About