High impact information on RCJMB04_24e12

• The three crystallins, alpha B-crystallin, tau-crystallin/alpha-enolase and epsilon-crystallin/lactate dehydrogenase B are all stress induced proteins and may thus share common regulatory elements [1].
• Whereas alpha-enolase was the predominant carbonyl-reactive species among the water-soluble muscle proteins, several other proteins (actin, heat shock protein 70, and creatine kinase) contained carbonyls and/or 3-nitrotyrosine [2].
• The amino acid sequence between residues 33 and 50 in chicken alpha-enolase coincided with the reported tryptic peptide sequence of rabbit beta-enolase, the tyrosine residue in which was phosphorylated in vitro by Rous-sarcoma-virus tyrosine kinase [3].
• In skeletal muscle, complete switching from alpha alpha enolase to beta beta was observed during the period around hatching [4].

Biological context of RCJMB04_24e12

• The deduced amino acid sequence of the chicken alpha-enolase showed more than 90% homologies with those of other vertebrate alpha-enolases including amphibian (Xenopus laevis) alpha-like enolase [3].
• Northern blot analysis indicated that alpha-enolase mRNA can be expressed in a wide range of chicken tissues, and that the gene expression switch from alpha to beta-enolase occurs just after hatching in developing chicken muscle [3].
• Chicken alpha-enolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis [3].

Anatomical context of RCJMB04_24e12

• Enolase of the chicken lens epithelium was found to be an enzymatically active dimeric protein of molecular weight 100,000 daltons and representing alpha-enolase [5].

Analytical, diagnostic and therapeutic context of RCJMB04_24e12

• We demonstrate that tau-crystallin/alpha-enolase and triose phosphate isomerase (TIM) are among the major proteins expressed in the crocodile cornea as resolved by 2D gel electrophoresis and identified by MALDI-TOF [6].

References