The Experts below are selected from a list of 97524 Experts worldwide ranked by ideXlab platform
Robert L Van Etten - One of the best experts on this subject based on the ideXlab platform.
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Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
Clinica Chimica Acta, 2002Co-Authors: Abdul Waheed, Robert L Van EttenAbstract: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.
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Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
Clinica Chimica Acta, 2002Co-Authors: Abdul Waheed, Robert L Van EttenAbstract: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.
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Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
Clinica Chimica Acta, 2002Co-Authors: Abdul Waheed, Robert L Van EttenAbstract: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.
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Protection of prostatic Acid Phosphatase activity in human serum samples by plasmin inhibitors.
Clinica Chimica Acta, 2002Co-Authors: Abdul Waheed, Robert L Van EttenAbstract: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.
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Prostatic Acid Phosphatase, a neglected ectonucleotidase
Purinergic Signalling, 2009Co-Authors: Herbert ZimmermannAbstract: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.
Lukasz Lebioda - One of the best experts on this subject based on the ideXlab platform.
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Structural Origins of l(+)-Tartrate Inhibition of Human Prostatic Acid Phosphatase
Journal of Biological Chemistry, 1998Co-Authors: Michael W. Lacount, George Handy, Lukasz LebiodaAbstract:Acid Phosphatase activity in the blood serum is usually separated into tartrate-resistant and tartrate-refractory, which is reported as the prostatic Acid Phosphatase level. Human prostatic Acid Phosphatase crystals soaked in N-propyl-L-tartramate were used to collect x-ray diffraction data to 2.9 A resolution under cryogenic conditions. Positive difference electron density, corresponding to the inhibitor, was found. The quality of the electron density maps clearly shows the orientation of the carboxylate and N-propyl-substituted amide groups. The hydroxyl group attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257. Previous crystallographic studies compiled on the tartrate-rat prostatic Acid Phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned D-tartrate into the active site. Modeling studies have shown that the C3 hydroxyl group on the D(-)-stereoisomer of tartrate, which does not significantly inhibit prostatic Acid Phosphatase, does not form strong hydrogen bonds with Arg-79 or His-257. The structure of human prostatic Acid Phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to develop inhibitors with higher specificity and potency than L(+)-tartrate.
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structural origins of l tartrate inhibition of human prostatic Acid Phosphatase
Journal of Biological Chemistry, 1998Co-Authors: Michael W. Lacount, George Handy, Lukasz LebiodaAbstract:Acid Phosphatase activity in the blood serum is usually separated into tartrate-resistant and tartrate-refractory, which is reported as the prostatic Acid Phosphatase level. Human prostatic Acid Phosphatase crystals soaked in N-propyl-L-tartramate were used to collect x-ray diffraction data to 2.9 A resolution under cryogenic conditions. Positive difference electron density, corresponding to the inhibitor, was found. The quality of the electron density maps clearly shows the orientation of the carboxylate and N-propyl-substituted amide groups. The hydroxyl group attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257. Previous crystallographic studies compiled on the tartrate-rat prostatic Acid Phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned D-tartrate into the active site. Modeling studies have shown that the C3 hydroxyl group on the D(-)-stereoisomer of tartrate, which does not significantly inhibit prostatic Acid Phosphatase, does not form strong hydrogen bonds with Arg-79 or His-257. The structure of human prostatic Acid Phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to develop inhibitors with higher specificity and potency than L(+)-tartrate.
Michael W. Lacount - One of the best experts on this subject based on the ideXlab platform.
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Structural Origins of l(+)-Tartrate Inhibition of Human Prostatic Acid Phosphatase
Journal of Biological Chemistry, 1998Co-Authors: Michael W. Lacount, George Handy, Lukasz LebiodaAbstract:Acid Phosphatase activity in the blood serum is usually separated into tartrate-resistant and tartrate-refractory, which is reported as the prostatic Acid Phosphatase level. Human prostatic Acid Phosphatase crystals soaked in N-propyl-L-tartramate were used to collect x-ray diffraction data to 2.9 A resolution under cryogenic conditions. Positive difference electron density, corresponding to the inhibitor, was found. The quality of the electron density maps clearly shows the orientation of the carboxylate and N-propyl-substituted amide groups. The hydroxyl group attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257. Previous crystallographic studies compiled on the tartrate-rat prostatic Acid Phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned D-tartrate into the active site. Modeling studies have shown that the C3 hydroxyl group on the D(-)-stereoisomer of tartrate, which does not significantly inhibit prostatic Acid Phosphatase, does not form strong hydrogen bonds with Arg-79 or His-257. The structure of human prostatic Acid Phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to develop inhibitors with higher specificity and potency than L(+)-tartrate.
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structural origins of l tartrate inhibition of human prostatic Acid Phosphatase
Journal of Biological Chemistry, 1998Co-Authors: Michael W. Lacount, George Handy, Lukasz LebiodaAbstract:Acid Phosphatase activity in the blood serum is usually separated into tartrate-resistant and tartrate-refractory, which is reported as the prostatic Acid Phosphatase level. Human prostatic Acid Phosphatase crystals soaked in N-propyl-L-tartramate were used to collect x-ray diffraction data to 2.9 A resolution under cryogenic conditions. Positive difference electron density, corresponding to the inhibitor, was found. The quality of the electron density maps clearly shows the orientation of the carboxylate and N-propyl-substituted amide groups. The hydroxyl group attached to C3 forms two crucial hydrogen bonds with Arg-79 and His-257. Previous crystallographic studies compiled on the tartrate-rat prostatic Acid Phosphatase binary complex (Lindqvist, Y., Schneider, G., and Vihko, P. (1993) J. Biol. Chem. 268, 20744-20746) erroneously positioned D-tartrate into the active site. Modeling studies have shown that the C3 hydroxyl group on the D(-)-stereoisomer of tartrate, which does not significantly inhibit prostatic Acid Phosphatase, does not form strong hydrogen bonds with Arg-79 or His-257. The structure of human prostatic Acid Phosphatase, noncovalently bound in N-propyl-L-tartramate, is used to develop inhibitors with higher specificity and potency than L(+)-tartrate.
