Clinical Chemistry
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Clinical Chemistry 24: 1525-1530, 1978;
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Clinical Chemistry, Vol 24, 1525-1530, Copyright © 1978 by American Association for Clinical Chemistry

Selective purification of tartrate-inhibitable acid phosphatases: rapid and efficient purification (to homogeneity) of human and canine prostatic acid phosphatases

RL Van Etten and MS Saini

We describe the synthesis of a long-chain monoamide derivative of L(+)- tartaric acid and its attachment to Sepharose 4B. Procedures are then described for use of this material in purifying human prostatic and (for the first time) canine prostatic acid phosphatases to constant specific activity and electrophoretic homogeneity. Depending on sample size, such purification is possible in one step, and is clearly faster and more efficient than are previously described methods. These materials and procedures have significant potential in studies of the comparative biochemistry and clinical chemistry of tartrateinhibitable acid phosphatases.


The following articles in journals at HighWire Press have cited this article:


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 J. Biol. Chem.Home page
M. W. LaCount, G. Handy, and L. Lebioda
Structural Origins of L(+)-Tartrate Inhibition of Human Prostatic Acid Phosphatase
J. Biol. Chem., November 13, 1998; 273(46): 30406 - 30409.
[Abstract] [Full Text] [PDF]

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J. Myers and T. Widlanski
Mechanism-based inactivation of prostatic acid phosphatase
Science, November 26, 1993; 262(5138): 1451 - 1453.
[Abstract] [PDF]

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 Cold Spring Harb Symp Quant BiolHome page
J. Dodd, C.E. Jahr, P.N. Hamilton, M.J.S. Heath, W.D. Matthew, and T.M. Jessell
Cytochemical and Physiological Properties of Sensory and Dorsal Horn Neurons That Transmit Cutaneous Sensation
Cold Spring Harb Symp Quant Biol, January 1, 1983; 48(0): 685 - 695.
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Copyright © 1978 by the American Association for Clinical Chemistry.