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Acid Phosphatase

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Robert L Van Etten – One of the best experts on this subject based on the ideXlab platform.

  • Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
    Clinica Chimica Acta, 2002
    Co-Authors: Abdul Waheed, Robert L Van Etten

    Abstract:

    Background: The level of prostatic Acid Phosphatase in serum is an established marker for prostate carcinoma. Methods: Inactivation of homogeneous prostatic Acid Phosphatase from human seminal fluid by purified plasmin and human serum was studied in the presence and absence of bovine pancreatic trypsin inhibitor, a plasmin inhibitor, or phenylmethylsulfonylfluoride, a serine protease inhibitor. Results: Plasmin or serine protease inhibitors protect against prostatic Acid Phosphatase inactivation in serum samples. Conclusion: The immediate addition of serine protease inhibitors to serum samples taken for prostatic Acid Phosphatase determinations should provide more accurate results and permit extended storage of samples. The stabilization of the enzyme activity and immunological properties of prostatic Acid Phosphatase in blood samples by these protease inhibitors resurrects the clinical significance of prostatic Acid Phosphatase measurements in prostate cancer screenings.

  • Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
    Clinica Chimica Acta, 2002
    Co-Authors: Abdul Waheed, Robert L Van Etten

    Abstract:

    The level of prostatic Acid Phosphatase in serum is an established marker for prostate carcinoma.
    Inactivation of homogeneous prostatic Acid Phosphatase from human seminal fluid by purified plasmin and human serum was studied in the presence and absence of bovine pancreatic trypsin inhibitor, a plasmin inhibitor, or phenylmethylsulfonylfluoride, a serine protease inhibitor.
    Plasmin or serine protease inhibitors protect against prostatic Acid Phosphatase inactivation in serum samples.
    The immediate addition of serine protease inhibitors to serum samples taken for prostatic Acid Phosphatase determinations should provide more accurate results and permit extended storage of samples. The stabilization of the enzyme activity and immunological properties of prostatic Acid Phosphatase in blood samples by these protease inhibitors resurrects the clinical significance of prostatic Acid Phosphatase measurements in prostate cancer screenings.

Abdul Waheed – One of the best experts on this subject based on the ideXlab platform.

  • Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
    Clinica Chimica Acta, 2002
    Co-Authors: Abdul Waheed, Robert L Van Etten

    Abstract:

    Background: The level of prostatic Acid Phosphatase in serum is an established marker for prostate carcinoma. Methods: Inactivation of homogeneous prostatic Acid Phosphatase from human seminal fluid by purified plasmin and human serum was studied in the presence and absence of bovine pancreatic trypsin inhibitor, a plasmin inhibitor, or phenylmethylsulfonylfluoride, a serine protease inhibitor. Results: Plasmin or serine protease inhibitors protect against prostatic Acid Phosphatase inactivation in serum samples. Conclusion: The immediate addition of serine protease inhibitors to serum samples taken for prostatic Acid Phosphatase determinations should provide more accurate results and permit extended storage of samples. The stabilization of the enzyme activity and immunological properties of prostatic Acid Phosphatase in blood samples by these protease inhibitors resurrects the clinical significance of prostatic Acid Phosphatase measurements in prostate cancer screenings.

  • Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
    Clinica Chimica Acta, 2002
    Co-Authors: Abdul Waheed, Robert L Van Etten

    Abstract:

    The level of prostatic Acid Phosphatase in serum is an established marker for prostate carcinoma.
    Inactivation of homogeneous prostatic Acid Phosphatase from human seminal fluid by purified plasmin and human serum was studied in the presence and absence of bovine pancreatic trypsin inhibitor, a plasmin inhibitor, or phenylmethylsulfonylfluoride, a serine protease inhibitor.
    Plasmin or serine protease inhibitors protect against prostatic Acid Phosphatase inactivation in serum samples.
    The immediate addition of serine protease inhibitors to serum samples taken for prostatic Acid Phosphatase determinations should provide more accurate results and permit extended storage of samples. The stabilization of the enzyme activity and immunological properties of prostatic Acid Phosphatase in blood samples by these protease inhibitors resurrects the clinical significance of prostatic Acid Phosphatase measurements in prostate cancer screenings.

Herbert Zimmermann – One of the best experts on this subject based on the ideXlab platform.

  • Prostatic Acid Phosphatase, a neglected ectonucleotidase
    Purinergic Signalling, 2009
    Co-Authors: Herbert Zimmermann

    Abstract:

    Two recent papers reveal that the soluble and secreted prostatic Acid Phosphatase, an enzyme that has long served as a diagnostic marker for prostate cancer, has a membrane-bound splice variant. This enzyme exhibits ecto-5′-nucleotidase activity, is widely distributed, and implicated in the formation of chronic pain. While prostatic Acid Phosphatase hydrolyzes phosphomonoesters other than 5′-nucleoside monophosphates these novel data suggest that, in addition to ecto-5′-nucleotidase and the alkaline Phosphatases, prostatic Acid Phosphatase must be taken into account in future studies on extracellular adenosine production.