Results 181 to 190 of about 43,806 (240)
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The multifaceted roles of Leptospira enolase
Research in Microbiology, 2017A previous study had demonstrated that Leptospira enolase is secreted extracellularly by a yet unknown mechanism and reassociates with the bacterial membrane. Surface-anchored leptospiral enolase displays plasminogen binding activity. In this work, we explored the consequences of this interaction and also assessed whether Leptospira enolase might ...
Angela Barbosa
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Urological Research, 1990
We determined concentrations of alpha and gamma-enolases in normal testis and in seminoma tissues by enzyme immunoassay. Concentrations of alpha-enolase were 4,170 +/- 2,040 ng/mg protein in normal testis (n = 8) and 8,140 +/- 4,480 ng/mg protein in seminoma (n = 8).
M, Takashi +4 more
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We determined concentrations of alpha and gamma-enolases in normal testis and in seminoma tissues by enzyme immunoassay. Concentrations of alpha-enolase were 4,170 +/- 2,040 ng/mg protein in normal testis (n = 8) and 8,140 +/- 4,480 ng/mg protein in seminoma (n = 8).
M, Takashi +4 more
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Biochimica et Biophysica Acta (BBA) - Protein Structure, 1973
Contrary to previous reports, yeast enolase was found to contain one cysteine per subunit (44 000 mol. wt). These residues do not readily react with 5,5′-dithiobis-(2-nitrobenzoic acid) except in 8 M urea suggesting the cysteines are “buried” within the subunits, 5,5′-Dithiobis-(2-nitrobenzoic acid) or Hg2+ prevent recovery of enzyme activity normally ...
S K, O, J, Travis, J M, Brewer
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Contrary to previous reports, yeast enolase was found to contain one cysteine per subunit (44 000 mol. wt). These residues do not readily react with 5,5′-dithiobis-(2-nitrobenzoic acid) except in 8 M urea suggesting the cysteines are “buried” within the subunits, 5,5′-Dithiobis-(2-nitrobenzoic acid) or Hg2+ prevent recovery of enzyme activity normally ...
S K, O, J, Travis, J M, Brewer
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Analysis of the Thermostability of Enolases
1976We have previously (1,2) characterized the enolases purified from the thermophiles Thermus X-1 and Thermus aquaticus YT-1. In this report we wish to establish the homology of these enzymes with enolases purified from two mesophilic organisms, yeast and rabbit, to illustrate the variability of thermostability measured by a variety of procedures, and to ...
E, Stellwagen, L D, Barnes
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The Saccharomyces cerevisiae enolase‐related regions encode proteins that are active enolases
Yeast, 2013AbstractIn addition to two genes (ENO1 and ENO2) known to code for enolase (EC4.2.1.11), the Saccharomyces cerevisiae genome contains three enolase‐related regions (ERR1, ERR2 and ERR3) which could potentially encode proteins with enolase function. Here, we show that products of these genes (Err2p and Err3p) have secondary and quaternary structures ...
Kornblatt, M +6 more
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Enolase in the avian and turtle lens
Current Eye Research, 1990Enolase is a dimeric enzyme of molecular weight of 100,000 daltons, which plays an important role in the glycolytic cycle. The aim of this study was to characterize the enzyme of the chicken lens epithelium and to compare its distribution in different regions of the chicken, duck and turtle lens.
G, Rudner, M, Katar, H, Maisel
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Inactivation of yeast enolase with tetranitromethane
Biochemical and Biophysical Research Communications, 1982Abstract Yeast enolase is inactivated by tetranitromethane with production of 1.2 moles of nitrotyrosine per subunit. Protection is afforded by “conformational” metal ion alone. Enzyme thus inactivated no longer appears to bind “conformational” metal ion.
S G, Spencer, J M, Brewer
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Lobster enolase crystallized by serendipity
Proteins: Structure, Function, and Bioinformatics, 1994AbstractAn unknown protein crystallized from a lobster muscle preparation in which arginine kinase was the majority component. It was identified as enolase by peptide sequencing and activity testing, and a SIRAS electron density map showed its three‐dimensional structure to be very similar to that of yeast enolase. © 1994 John Wiley & Sons, Inc.
S, Duquerroy, G, Le Bras, J, Janin
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The Role of Enolases in Allergic Disease
The Journal of Allergy and Clinical Immunology: In Practice, 2021Enolase is one of the most abundant cytosolic enzymes as well as an important glycolytic metalloenzyme highly conserved among organisms from different taxonomical groups. Participation of enolase in processes in which its enzymatic activity is not required has been widely reported.
Martha Beatriz, Morales-Amparano +3 more
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