Comparative studies of rat recombinant purple acid phosphatase and bone tartrate-resistant acid phosphatase

Expression of tartrate-resistant acid phosphatase.

Tartrate-resistant acid phosphatase as a marker of bone resorption.

Tartrate-resistant serum acid phosphatase was measured in 123 subjects, 80 of which were normal and the rest pathologic, in order to define the profile and value of this parameter as a biological marker of osteoclastic activity. Normal subjects were divided into age groups based on the period where skeletal growth ends (under 20 years), at the age of menopause in women (50 years, between 20 and...

Enzyme immunoassay for tartrate-resistant acid phosphatase.

An immunochemical method for quantitative analysis of the tartrate-resistant acid phosphatase (EC 3.1.3.2), band 5, is presented. This method involves precipitation of the enzyme from the serum by the antibody specific to band 5 and by sheep anti-rabbit immunoglobulin, followed by analysis of the enzyme activity in the precipitate. The precipitation procedure eliminates the interferences of the...

Cloning, sequence, and developmental expression of a type 5, tartrate-resistant, acid phosphatase of rat bone.

Tartrate-resistant acid phosphatase (TRAP) is a characteristic constituent of osteoclasts and some mononuclear preosteoclasts and, therefore, used as a histochemical and biochemical marker for osteoclasts and bone resorption. We now report the isolation of a 1397-base pair (bp) full-length TRAP/tartrate-resistant acid ATPase (TrATPase) cDNA clone from a neonatal rat calvaria lambda gt11 cDNA li...

Tartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinases.

Purple acid phosphatases (PAPs) are binuclear acid metallohydrolases also referred to as tartrate-resistant acid phosphatases (TRAPs) or type 5 acid phosphatases. The cDNA sequences of TRAP/PAP enzymes from different species and organs indicate that these enzymes are translated as monomeric polypeptides of approx. 35 kDa, contrasting with the predominantly two-subunit structure observed in puri...