Acid phosphatases in mammalian tissues. Evidence for the existence of a 57 kDa Zn(2+)-dependent acid phosphatase form.
1. A comparative study of multiple forms of acid phosphatase (AcPase) in various organs of mammals was carried out. 2. These studies indicated that the high-molecular weight AcPase is preferentially expressed by tissues which undergo cell proliferation such as epithelial tissues; on the contrary, the low-molecular weight enzyme seems to be characteristic of highly differentiated tissues such as nervous, muscle and blood erythrocytes. 3. The existence of a new AcPase activated by Zn2+ ions was observed in all tissues studied with the exception of erythrocytes. 4. The enzyme shows a molecular weight of 57 kDa, is insensitive to NaF, hydrolyzes p-nitro-phenylphosphate and o-c-phenylphosphate; ATP, a-naphthyl-phosphate and beta-glycerolphosphate are also dephosphorylated.
Panara
F
F
Instituto di Anatomia Comparata, Facoltà di Scienze MM.FF.NN., Università di Perugia, Italia.
Angiolillo
A
A
Fagotti
A
A
Di Rosa
I
I
Francesca
S
S
Pascolini
R
R
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D002413:Cations, Divalent; D002417:Cattle; D002850:Chromatography, Gel; D004789:Enzyme Activation; D006801:Humans; D008322:Mammals; D051381:Rats; D014018:Tissue Distribution; D015032:Zinc / Q000378:metabolism*
D002413:Cations, Divalent; D000135:Acid Phosphatase; D015032:Zinc