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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todo:paper_00032697_v179_n1_p56_Murray2023-10-03T13:55:48Z A radioactive method for the measurement of trypsin and trypsin-like activities Murray, P.F. Silberstein, S. Cantore, M.L. Passeron, S. 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. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar 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 Murray, P.F. Silberstein, S. Cantore, M.L. Passeron, S. 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. |
| format |
JOUR |
| author |
Murray, P.F. Silberstein, S. Cantore, M.L. Passeron, S. |
| author_facet |
Murray, P.F. Silberstein, S. Cantore, M.L. Passeron, S. |
| author_sort |
Murray, P.F. |
| 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 |
| url |
http://hdl.handle.net/20.500.12110/paper_00032697_v179_n1_p56_Murray |
| work_keys_str_mv |
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| _version_ |
1807317749904441344 |