Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. When rabbit muscle aldolase labelled with tritium and inactivated by N-ethylmaleimide (NEM) was loaded into erythrocyte ghosts, significant proteolysis of the loaded protein occurred. The major product of this proteolysis, separated by electrophoresis under dissociating conditions, was found to be approx. 2 kDa smaller than the parent protein. 2. Proteolysis was detectable during erythrocyte ghost loading at 0 degrees C, reaching a plateau after approx. 12 min. Subsequent incubation at 37 degrees C to allow resealing of the ghosts resulted in additional proteolysis, and up to 20% of the loaded protein was converted to the smaller 38 kDa derivative. 3. EDTA, EGTA, leupeptin and chymostatin, each inhibitors of calcium-activated neutral proteinases (calpains), were the most effective inhibitors of the proteolysis of NEM-inactivated aldolase in ghosts. Other proteinase inhibitors were ineffective, while phenylmethanesulphonyl fluoride was only partially effective. 4. Inhibition of the proteolysis by EGTA was prevented by CaCl2, supporting the involvement of erythrocyte calpain. 5. Pretreatment of ghosts with EGTA prior to loading of NEM-modified aldolase followed by microinjection of the protein into HeLa cells did not result in a different rate of its overall breakdown to acid-soluble products. EGTA is suggested as a useful agent for the erythrocyte ghost-mediated microinjection of calpain-sensitive proteins.
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PMID:Proteolysis of N-ethylmaleimide-modified aldolase loaded into erythrocyte ghosts: prevention by inhibitors of calpain. 254 83

The effect of exercise on the binding of glycolytic enzymes to subcellular structures was examined in rainbow trout (Salmo gardneri). Both "burst" and "endurance" type exercise produced an increase of approximately 50% in the percentage of phosphofructokinase (PFK), glyceraldehyde 3-phosphate dehydrogenase (GAPDH), aldolase, and 3-phosphoglycerate kinase associated with particulate matter in white skeletal muscle. In contrast, cardiac muscle showed no change in enzyme binding when trout were exercised, suggesting that the effects seen in white muscle are related to an increased anaerobic glycolytic flux in this tissue. Modulation of binding by altered pH or calcium ion concentration was tested: a decrease in pH increased PFK binding to subcellular particles, whereas 2 mM CaCl2 decreased GAPDH binding. These results are discussed with respect to the formation of a glycolytic complex during exercise in trout white muscle.
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PMID:Subcellular enzyme binding in glycolytic control: in vivo studies with fish muscle. 340 3