Glycation of myofibrillar proteins and ATPase activity after incubation with eleven sugars.
Rat skeletal muscle myofibrils were incubated in the presence of D-glucose, D-fructose, D-galactose, D-ribose, D-tagatose, D-arabinose, D-xylose, D-mannose, L-sorbose, L-rhamnose or DL-glyceraldehyde and myofibrillar ATPase activity as well as the extent of glycation was measured. The attachment of sugars to proteins during glycation was generally dependent on the percentage of a given sugar present in the open-chain form. Glycation resulted in the decrease of myofibrillar ATPase activity. This decrease was low after incubation of myofibrillar proteins with slowly glycating sugars (e.g. glucose) and high with fast glycating sugars (e.g. ribose or glyceraldehyde). ATPase activity was less reduced in the presence of beta-mercaptoethanol.
Syrový
I
I
Institute of Physiology, Academy of Sciences of the Czech Republic, Prague.
D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D050260:Carbohydrate Metabolism; D002241:Carbohydrates / Q000494:pharmacology; D006023:Glycoproteins / Q000096:biosynthesis*; D066298:In Vitro Techniques; D008623:Mercaptoethanol / Q000494:pharmacology; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism; D009210:Myofibrils / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D017392:Thiobarbituric Acid Reactive Substances / Q000378:metabolism
D002241:Carbohydrates; D006023:Glycoproteins; D009124:Muscle Proteins; D017392:Thiobarbituric Acid Reactive Substances; D008623:Mercaptoethanol; D017301:Ca(2+) Mg(2+)-ATPase