A lead conversion method for staining thiamine pyrophosphatase and other phosphatases in rat brain after thin layer polyacrylamide gel isoelectric focusing.
Rat brain thiamine pyrophosphatase (TPPase) was separated by thin layer polyacrylamide gel isoelectric focusing (IF) and stained with a modification of the lead conversion method of Allen and Hyncik (1963). 10 bands with TPPase activity were observed in the pH range 4.6-7.1. The overall IF pattern of TPPase was similar to that of uridine diphosphatase and inosine diphosphatase but was clearly different from that of adenosine diphosphatase, p-nitrophenyl phosphatase, alpha-naphthyl phosphatase and thiamine monophosphatase. A semiquantitative assessment of TPPase isoenzymes has been performed using laser densitometry.
Mazzarello
P
P
Clinica Neurologica I, Università di Milano, Italy.
Poloni
M
M
Patrini
C
C
Bosone
D
D
Rindi
G
G
D000818:Animals; D001921:Brain / Q000201:enzymology*; D005260:Female; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis*; D007854:Lead; D008297:Male; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D011755:Pyrophosphatases / Q000032:analysis*; D051381:Rats; D011919:Rats, Inbred Strains; D013194:Staining and Labeling; D013834:Thiamine Pyrophosphatase / Q000032:analysis*
D007527:Isoenzymes; D007854:Lead; D010744:Phosphoric Monoester Hydrolases; D011755:Pyrophosphatases; D013834:Thiamine Pyrophosphatase