High impact information on ENO1

• Reproducible survival of adult pig rod and cone photoreceptors was obtained for approximately 2 weeks in vitro, with the continued expression of rod opsin, recoverin, S-antigen, cone arrestin, and neuron-specific enolase [1].
• Neuron-specific enolase and S-100 protein immunohistochemistry for defining the structure and topographical relationship of the different enteric nerve plexuses in the small intestine of the pig [2].
• Neuron-specific enolase-like immunoreactivity in inner hair cells but not outer hair cells in the guinea pig organ of Corti [3].
• Concentrations of total proteins, the light subunit of the neurofilament protein, S-100 protein, neuron-specific enolase, and glial fibrillary acidic protein were measured, and the presence of oligoclonal bands (immunoglobulins) were assayed in cerebrospinal fluid [4].
• Despite these physical and chemical differences, the kinetic constants [KM values for Mg2+, 2-phosphoglyceric acid, and phospho(enol)pyruvate] appear not to be significantly different for these two forms of enolase [5].

Biological context of ENO1

• The possible physiological role of enolase in carbohydrate metabolism is discussed [6].

Associations of ENO1 with chemical compounds

• The two enzymes differ in their content of lysine [liver enolase (L) = 94 residues, muscle enolase (M) = 68 residues], histidine (L = 13, M = 21), serine (L = 53, M = 36), proline (L = 52, M = 34), and cysteine (L = 4, M = 21) [5].
• There were no intergroup differences regarding glial fibrillary acidic protein, neuron-specific enolase, S-100, interleukin-8, or substance P endopeptidase activity [7].
• The native dimeric form of enolase from pig muscle was immobilized on Sepharose 4B activated with cyanogen bromide [8].
• This treatment resulted in an increased degree of binding of all the glycolytic enzymes, but with the most marked increases occurring with phosphofructokinase, enolase and pyruvate kinase [9].

Analytical, diagnostic and therapeutic context of ENO1

• SDS-PAGE experiments give a molecular weight value of 46,000 D for liver enolase and a value of 44,000 D for muscle enolase [5].
• Immobilization of pig muscle enolase. Studies on the activity of subunits [8].
• Only on the Sepharose activated with small quantities of CNBr the amount of protein which remained after treatment with Gdn.HCl was about 50% of the initially bound enolase, indicating that the enzyme was bound covalently to the matrix through a single subunit [8].
• After 1 week, 6 mL of cerebrospinal fluid was collected, and four structural nerve proteins, neurofilaments, S-100, glial fibrillary acidic protein, neuron-specific enolase, the proinflammatory cytokine interleukin-8, the neurotransmitter nociceptin, and substance P endopeptidase activity were analyzed using immunoassays [7].

References