A radioactive method for the measurement of trypsin and trypsin-like activities

A simple and highly sensitive method for the assay of trypsin has been developed by making use of the phosphorylated synthetic peptide Leu-Arg-Arg-Ala-Ser-(32P)-Leu-Gly as substrate. The technique has been adapted from the phosphocellulose method of R. Roskoski, Jr. (in Methods in Enzymology (Corbin...

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Detalles Bibliográficos
Autores principales: Silberstein Cuña, Susana Iris, Cantore de Ezcurra, María Leonor
Publicado: 1989
Materias:
peptidase
radioisotope
trypsin
enzyme assay
methodology
priority journal
radioassay
saccobolus platensis
Adenosine Triphosphate
Amino Acid Sequence
Ascomycota
Hydrogen-Ion Concentration
Peptide Hydrolases
Phosphorus Radioisotopes
Phosphorylation
Support, Non-U.S. Gov't
Trypsin
Trypsin Inhibitors
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v179_n1_p56_Murray
http://hdl.handle.net/20.500.12110/paper_00032697_v179_n1_p56_Murray
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
id paper:paper_00032697_v179_n1_p56_Murray
record_format dspace
spelling paper:paper_00032697_v179_n1_p56_Murray2023-06-08T14:24:00Z A radioactive method for the measurement of trypsin and trypsin-like activities Silberstein Cuña, Susana Iris Cantore de Ezcurra, María Leonor peptidase radioisotope trypsin enzyme assay methodology priority journal radioassay saccobolus platensis Adenosine Triphosphate Amino Acid Sequence Ascomycota Hydrogen-Ion Concentration Peptide Hydrolases Phosphorus Radioisotopes Phosphorylation Support, Non-U.S. Gov't Trypsin Trypsin Inhibitors A simple and highly sensitive method for the assay of trypsin has been developed by making use of the phosphorylated synthetic peptide Leu-Arg-Arg-Ala-Ser-(32P)-Leu-Gly as substrate. The technique has been adapted from the phosphocellulose method of R. Roskoski, Jr. (in Methods in Enzymology (Corbin, J., and Hardman, J., Eds.), Vol. 99, pp. 3-6, Academic Press, New York) used for measuring of protein kinases. In addition to measuring the activity of trypsin at the microgram level, the 32P-labeled peptide method can be used for measuring other trypsin-like enzymes. It has been successfully utilized for the identification of a new peptidase from the fungus Saccobolus platensis. © 1989. Fil:Silberstein, S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Cantore, M.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1989 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v179_n1_p56_Murray http://hdl.handle.net/20.500.12110/paper_00032697_v179_n1_p56_Murray
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic peptidase
radioisotope
trypsin
enzyme assay
methodology
priority journal
radioassay
saccobolus platensis
Adenosine Triphosphate
Amino Acid Sequence
Ascomycota
Hydrogen-Ion Concentration
Peptide Hydrolases
Phosphorus Radioisotopes
Phosphorylation
Support, Non-U.S. Gov't
Trypsin
Trypsin Inhibitors
spellingShingle peptidase
radioisotope
trypsin
enzyme assay
methodology
priority journal
radioassay
saccobolus platensis
Adenosine Triphosphate
Amino Acid Sequence
Ascomycota
Hydrogen-Ion Concentration
Peptide Hydrolases
Phosphorus Radioisotopes
Phosphorylation
Support, Non-U.S. Gov't
Trypsin
Trypsin Inhibitors
Silberstein Cuña, Susana Iris
Cantore de Ezcurra, María Leonor
A radioactive method for the measurement of trypsin and trypsin-like activities
topic_facet peptidase
radioisotope
trypsin
enzyme assay
methodology
priority journal
radioassay
saccobolus platensis
Adenosine Triphosphate
Amino Acid Sequence
Ascomycota
Hydrogen-Ion Concentration
Peptide Hydrolases
Phosphorus Radioisotopes
Phosphorylation
Support, Non-U.S. Gov't
Trypsin
Trypsin Inhibitors
description A simple and highly sensitive method for the assay of trypsin has been developed by making use of the phosphorylated synthetic peptide Leu-Arg-Arg-Ala-Ser-(32P)-Leu-Gly as substrate. The technique has been adapted from the phosphocellulose method of R. Roskoski, Jr. (in Methods in Enzymology (Corbin, J., and Hardman, J., Eds.), Vol. 99, pp. 3-6, Academic Press, New York) used for measuring of protein kinases. In addition to measuring the activity of trypsin at the microgram level, the 32P-labeled peptide method can be used for measuring other trypsin-like enzymes. It has been successfully utilized for the identification of a new peptidase from the fungus Saccobolus platensis. © 1989.
author Silberstein Cuña, Susana Iris
Cantore de Ezcurra, María Leonor
author_facet Silberstein Cuña, Susana Iris
Cantore de Ezcurra, María Leonor
author_sort Silberstein Cuña, Susana Iris
title A radioactive method for the measurement of trypsin and trypsin-like activities
title_short A radioactive method for the measurement of trypsin and trypsin-like activities
title_full A radioactive method for the measurement of trypsin and trypsin-like activities
title_fullStr A radioactive method for the measurement of trypsin and trypsin-like activities
title_full_unstemmed A radioactive method for the measurement of trypsin and trypsin-like activities
title_sort radioactive method for the measurement of trypsin and trypsin-like activities
publishDate 1989
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v179_n1_p56_Murray
http://hdl.handle.net/20.500.12110/paper_00032697_v179_n1_p56_Murray
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AT cantoredeezcurramarialeonor aradioactivemethodforthemeasurementoftrypsinandtrypsinlikeactivities
AT silbersteincunasusanairis radioactivemethodforthemeasurementoftrypsinandtrypsinlikeactivities
AT cantoredeezcurramarialeonor radioactivemethodforthemeasurementoftrypsinandtrypsinlikeactivities
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