Abstract
Human prostatic acid phosphatase (EC: 3.1.3.2) belongs to the group of enzymes that can split simple phosphate esters, nucleotides, and phosphoamino acids in phosphoproteins including phosphotyrosine derivatives. The native phosphatase is a glycosylated homodimer with a molecular weight of 100kDa. Specific inhibition and denaturation-renaturation studies showed that the catalytic activity of the enzyme depends on the formation of the dimer. The enzyme is androgen-regulated and is a prostate-specific protein; and its level is often elevated in the blood serum of prostate cancer patients. Prostatic acid phosphatase can be stabilized against various denaturation agents by cross-linking techniques and can be used in different biomedical and biotechnological processes.
