Development and Characterization of Novel Monoclonal Antibodies Against Tartrate-Resistant Acid Phosphatase 5

Abstract We have characterized four monoclonal antibodies (mAbs) to the purple ("tartrate-resistant," band 5) acid phosphatase of the human osteoclast (TRAP) and used these to develop a specific serum immunoassay. All four mAbs are of high affinity (Ka = 1-5 x 10(8) L/mol) with a very fast Kassoc (0.2-2.0 x 10(5) L mol-1 s-1) and a moderate Kdissoc (1-3 x 10(-3) s). Two of the mAbs were selected to develop a time-resolved fluorescence immunoassay to measure serum concentrations of TRAP. The mean serum immunoreactive TRAP in a group of healthy premenopausal women and men was 3.7 +/- 1.8 micrograms/L (mean +/- SD) and 3.5 +/- 1.6 micrograms/L, respectively. Significantly higher concentrations of TRAP were found in postmenopausal women (6.3 +/- 2.3 micrograms/L) and in eight patients with Gaucher disease (19.3 +/- 4.7 micrograms/L). Further studies are required to investigate the value of serum TRAP as a marker of bone resorption.

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Characterization of Monoclonal Antibodies Specific to Human Tartrate-Resistant Acid Phosphatase

Hybridoma ◽

10.1089/hyb.1997.16.175 ◽

1997 ◽

Vol 16 (2) ◽

pp. 175-182 ◽

Cited By ~ 7

Author(s):

ANTHONY J. JANCKILA ◽

ERNEST M. CARDWELL ◽

LUNG T. YAM

Keyword(s):

Monoclonal Antibodies ◽

Acid Phosphatase ◽

Tartrate Resistant Acid Phosphatase

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Two-Site Immunoassays for Osteoclastic Tartrate-Resistant Acid Phosphatase Based on Characterization of Six Monoclonal Antibodies

Journal of Bone and Mineral Research ◽

10.1359/jbmr.1999.14.3.464 ◽

1999 ◽

Vol 14 (3) ◽

pp. 464-469 ◽

Cited By ~ 33

Author(s):

Jussi M. Halleen ◽

Matti Karp ◽

Sari Viloma ◽

Pirjo Laaksonen ◽

Jukka Hellman ◽

...

Keyword(s):

Monoclonal Antibodies ◽

Acid Phosphatase ◽

Tartrate Resistant Acid Phosphatase

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Characterization of Four Monoclonal Antibodies to Recombinant Human Tartrate-Resistant Acid Phosphatase

Hybridoma and Hybridomics ◽

10.1089/153685902760173917 ◽

2002 ◽

Vol 21 (3) ◽

pp. 191-195 ◽

Cited By ~ 3

Author(s):

Takashi Miyazaki ◽

Toshiyuki Matsunaga ◽

Shuichi Miyazaki ◽

Shigeru Hokari ◽

Tsugikazu Komoda

Keyword(s):

Monoclonal Antibodies ◽

Acid Phosphatase ◽

Tartrate Resistant Acid Phosphatase

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Biochemical characterization of the tartrate-resistant acid phosphatase of human spleen with leukemic reticuloendotheliosis as a pyrophosphatase.

Clinical Chemistry ◽

10.1093/clinchem/23.1.89 ◽

1977 ◽

Vol 23 (1) ◽

pp. 89-94 ◽

Cited By ~ 29

Author(s):

K W Lam ◽

L T Yam

Keyword(s):

Acid Phosphatase ◽

Biochemical Characterization ◽

Normal Animal ◽

Tartrate Resistant Acid Phosphatase ◽

Animal Tissues ◽

Human Spleen ◽

Optimal Activity ◽

Catalytic Function ◽

Hydrolysis Of

Abstract A tartrate-resistant acid phosphatase was isolated from a human leukemic spleen by freeze-thawing in saline and purified by repeated chromatography on carboxymethyl-cellulose. The purified enzyme has a molecular weight of 64 000. It catalyzes the hydrolysis of inorganic and organic pyrophosphate as well as the phenolic ester of monoorthophosphate, with optimal activity between pH 5 and 6. However, there is no activity toward mono-orthophosphate esters of aliphatic alcohols. The present data have identified its catalytic function as a pyrophosphatase. However, it has properties different from the pyrophosphatase previously observed in normal animal tissues.

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