The Experts below are selected from a list of 1380 Experts worldwide ranked by ideXlab platform
Rudolf Dernick - One of the best experts on this subject based on the ideXlab platform.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
Uwe Tessmer - One of the best experts on this subject based on the ideXlab platform.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
Folkert Donn - One of the best experts on this subject based on the ideXlab platform.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
Thomas Quack - One of the best experts on this subject based on the ideXlab platform.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
Astrid Leuner - One of the best experts on this subject based on the ideXlab platform.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.
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biological activity of prostate specific antigen isolated by sodium dodecyl sulfate polyacrylamide gel electrophoresis and electroelution
Electrophoresis, 1995Co-Authors: Uwe Tessmer, Folkert Donn, Astrid Leuner, Thomas Quack, Rudolf DernickAbstract:: Human prostate-specific antigen (PSA), a 33 kDa kallikrein-like serine protease, occurring in the prostate, in seminal plasma and in blood, was prepared under nonreducing conditions in an enzymatically active form from seminal plasma by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), followed by fast copper staining, electroelution from gel slices and dialysis against isotonic phosphate-buffered saline (PBS). Enzymatic activity was demonstrated for the first time directly by cleavage of semenogelin, one of the biological substrates of PSA, isolated by the same procedure, i.e. SDS-PAGE and electroelution, but from seminal vesicle fluid. The purified PSA formed SDS-stable complexes with the two major extracellular protease inhibitors in blood, Alpha 1-Antichymotrypsin (Alpha 1-ACH) and Alpha 2-macroglobulin (Alpha 2-M). PSA isolated under reducing conditions was enzymatically inactive and could not bind to the protease inhibitors Alpha 1-ACH and Alpha 2-M.