Results 191 to 200 of about 43,806 (240)

Comparative enzymology of molluscan enolases

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1971
1. 1. Enolases from five molluscs have been isolated and partially characterized. 2. 2. Michaelis constants, metal ion activation constants and molecular weights of molluscan enolases are typical of those obtained for enolases from a wide variety of sources. 3. 3.
D P, Hanlon, L, De Vore, M C, Kincaid, A, Jones, L, Lane   +4 more
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Structural and mechanistic studies of enolase

Current Opinion in Structural Biology, 1996
The high-resolution structure of yeast enolase cocrystallized with its equilibrium mixture of substrate and product reveals the stereochemistry of substrate/product binding and therefore the groups responsible for acid/base catalysis and stabilization of the enolate intermediate.
G H, Reed, R R, Poyner, T M, Larsen, J E, Wedekind, I, Rayment   +4 more
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Enolase isoenzymes in human gliomas

Journal of Neurosurgery, 1986
✓ Gamma-enolase (one of the three possible subunits of the dimeric enzyme enolase (EC 4.2.1.11)) has been reported as a marker for human neurons. Studies investigating the presence of γ-enolase in human gliomas have given conflicting results, but a definite finding is important for further studies of the biology of these tumors and the possible use of ...
E M, van den Doel, G, Rijksen, P J, Roholl, C W, van Veelen, G E, Staal   +4 more
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Rat brain enolase isozymes. Purification of three forms of enolase.

Journal of biochemistry, 1980
Three forms of rat brain enolase (Fletcher, L., Rider, C.C., & Taylor, C.B. (1976) Biochim. Biophys. Acta 452, 245-252), which were separable by DEAE-cellulose chromatography (referred as enolase I, enolase II, and enolase III in order of the elution), were purified with a high yield by use of column chromatographies of Sephadex G-150, Blue Sepharose ...
F, Suzuki, Y, Umeda, K, Kato
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Reaction intermediate analogs for enolase

Biochemistry, 1984
A number of compounds that appear to be analogues of the aci form of the normal carbanion intermediate are good inhibitors of yeast enolase. These include (3-hydroxy-2-nitropropyl)phosphonate (I), the ionized (pK = 8.1) nitronate form of which in the presence of 5 mM Mg2+ has a Ki of 6 nM, (nitroethyl)phosphonate (III) (pK = 8.5; Ki of the nitronate in
V E, Anderson, P M, Weiss, W W, Cleland
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Phosphonate analog substrates for enolase

Biochemistry, 1990
Phosphonate analogues in which the bridge between C-2 and phosphorus is a CH2 group are slow substrates for yeast enolase. The pH variation of the kinetic parameters for the methylene analogue of 2-phosphoglycerate suggests that the substrate binds as a dianion and that Mg2+ can bind subsequently only if a metal ligand and the catalytic base are ...
V E, Anderson, W W, Cleland
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Phosphorylation of Escherichia coli enolase

Biochimie, 1989
In vivo labeling of Escherichia coli JA200 pLC 11-8 resulted in 32P incorporation into enolase as demonstrated by immunoaffinity chromatography and electrophoresis followed by autoradiography. Complete acid hydrolysis, followed by thin layer chromatography was employed for determination of the phosphoamino acid residue.
H K, Dannelly, B, Duclos, A J, Cozzone, H C, Reeves   +3 more
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α-Enolase binds to RNA

Biochimie, 2011
To detect proteins binding to CUG triplet repeats, we performed magnetic bead affinity assays and North-Western analysis using a (CUG)(10) ssRNA probe and either nuclear or total extracts from rat L6 myoblasts. We report the isolation and identification by mass spectrometry and immunodetection of α-enolase, as a novel (CUG)n triplet repeat binding ...
Liliana, Hernández-Pérez, Francisco, Depardón, Fernando, Fernández-Ramírez, Alejandra, Sánchez-Trujillo, Rosa María, Bermúdez-Crúz, Lawrence, Dangott, Cecilia, Montañez   +6 more
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Enolase-1 as a plasminogen receptor

Blood, 2009
In this issue of Blood, Wygrecka and colleagues assign a major role to cell-surface enolase-1 as a plasminogen receptor, mediating LPS-induced invasion of monocytes into lungs in mice and humans.
Edward F, Plow, Riku, Das
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Enolase isozymes in Coho salmon

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1978
1. Analysis of the enolase isozymic distribution has been performed in tissues of the Coho salmon, using electrophoretic separation on cellulose acetate strips followed by localization of enzymatic activity. 2. A total of six electrophoretically distinct forms are seen in Coho salmon in patterns that differ both qualitatively and quantitatively from ...
S R, Landrey, R, Applegate, J M, Cardenas   +2 more
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