title: Post-mortem modifications of the specific activity of some brain enzymes.
abstract: 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.
authors.affiliation: Institute of Biological Chemistry, University of Florence, Italy.
authors.forename: G
authors.initials: G
authors.lastname: Liguri
authors.forename: P
authors.initials: P
authors.lastname: Nassi
authors.forename: N
authors.initials: N
authors.lastname: Taddei
authors.forename: C
authors.initials: C
authors.lastname: Nediani
authors.forename: G
authors.initials: G
authors.lastname: Ramponi
mesh_terms: 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*
chemical_list: D007770:L-Lactate Dehydrogenase; D006593:Hexokinase; D017301:Ca(2+) Mg(2+)-ATPase; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase