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P E Bock

Showing results (1-10 of 44) with videos related to

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The Journal of Biological Chemistry|July 25, 1992
Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinasesP E Bock
Biochemistry|August 23, 1988
Active site selective labeling of serine proteases with spectroscopic probes using thioester peptide chloromethyl ketones: demonstration of thrombin labeling using N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2ClP E Bock
The Journal of Biological Chemistry|July 25, 1992
Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. I. Specificity of thrombin labelingP E Bock
Methods in Enzymology|January 1, 1993
Thioester peptide chloromethyl ketones: reagents for active site-selective labeling of serine proteinases with spectroscopic probesP E Bock
The Journal of Biological Chemistry|September 25, 1976
Phosphofructokinase. I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzymeP E Bock, C Frieden
Biochemistry|September 24, 1974
pH-induced cold lability of rabbit skeletal muscle phosphofructokinaseP E Bock, C Frieden
The Journal of Biological Chemistry|September 25, 1976
Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzymeP E Bock, C Frieden
Analytical Biochemistry|November 1, 1983
Molecular weight of human high-molecular-weight kininogen light chain by equilibrium sedimentation in an air-driven ultracentrifugeP E Bock, H R Halvorson
Analytical Biochemistry|September 14, 2001
Biotin derivatives of D-Phe-Pro-Arg-CH2Cl for active-site-specific labeling of thrombin and other serine proteinasesP J Anderson, P E Bock
Biochemistry|November 15, 2000
Streptokinase binds preferentially to the extended conformation of plasminogen through lysine binding site and catalytic domain interactionsP D Boxrud, P E Bock
Pageof 5

Showing results (1-10 of 44) with videos related to

Sort By:
Pageof 5
The Journal of Biological Chemistry|July 25, 1992
Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. II. Properties of thrombin derivatives as reporters of prothrombin fragment 2 binding and specificity of the labeling approach for other proteinasesP E Bock
Biochemistry|August 23, 1988
Active site selective labeling of serine proteases with spectroscopic probes using thioester peptide chloromethyl ketones: demonstration of thrombin labeling using N alpha-[(acetylthio)acetyl]-D-Phe-Pro-Arg-CH2ClP E Bock
The Journal of Biological Chemistry|July 25, 1992
Active-site-selective labeling of blood coagulation proteinases with fluorescence probes by the use of thioester peptide chloromethyl ketones. I. Specificity of thrombin labelingP E Bock
Methods in Enzymology|January 1, 1993
Thioester peptide chloromethyl ketones: reagents for active site-selective labeling of serine proteinases with spectroscopic probesP E Bock
The Journal of Biological Chemistry|September 25, 1976
Phosphofructokinase. I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzymeP E Bock, C Frieden
Biochemistry|September 24, 1974
pH-induced cold lability of rabbit skeletal muscle phosphofructokinaseP E Bock, C Frieden
The Journal of Biological Chemistry|September 25, 1976
Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzymeP E Bock, C Frieden
Analytical Biochemistry|November 1, 1983
Molecular weight of human high-molecular-weight kininogen light chain by equilibrium sedimentation in an air-driven ultracentrifugeP E Bock, H R Halvorson
Analytical Biochemistry|September 14, 2001
Biotin derivatives of D-Phe-Pro-Arg-CH2Cl for active-site-specific labeling of thrombin and other serine proteinasesP J Anderson, P E Bock
Biochemistry|November 15, 2000
Streptokinase binds preferentially to the extended conformation of plasminogen through lysine binding site and catalytic domain interactionsP D Boxrud, P E Bock
Pageof 5