Post-mortem modifications of the specific activity of some brain enzymes.
The post-mortem stability of some brain enzymes was studied. Over the time period under examination, the cytoplasmic enzymes investigated underwent a decisive decay, hexokinase being the most labile and acylphosphatase the most stable. On the other hand, structured activities such as Na+, K+-ATPase and Ca2+, Mg2+-ATPase showed an apparent transitory increase. The differences in post-mortem stability of soluble enzymes could be ascribed, at least in part, to their different susceptibility toward proteolytic activities, as suggested by the electrophoretic results.
Liguri
G
G
Institute of Biological Chemistry, University of Florence, Italy.
Nassi
P
P
Taddei
N
N
Nediani
C
C
Ramponi
G
G
D000818:Animals; D001921:Brain / Q000201:enzymology*; D017301:Ca(2+) Mg(2+)-ATPase / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D006593:Hexokinase / Q000378:metabolism*; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008297:Male; D011180:Postmortem Changes; D051381:Rats; D011919:Rats, Inbred Strains; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D007770:L-Lactate Dehydrogenase; D006593:Hexokinase; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase