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.
Documento: | Artículo |
Título: | A radioactive method for the measurement of trypsin and trypsin-like activities |
Autor: | Murray, P.F.; Silberstein, S.; Cantore, M.L.; Passeron, S. |
Filiación: | Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Ciudad Universitaria, Pabellon II, 1428 Buenos Aires, Argentina |
Palabras clave: | 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 |
Año: | 1989 |
Volumen: | 179 |
Número: | 1 |
Página de inicio: | 56 |
Página de fin: | 59 |
DOI: | http://dx.doi.org/10.1016/0003-2697(89)90199-1 |
Título revista: | Analytical Biochemistry |
Título revista abreviado: | Anal. Biochem. |
ISSN: | 00032697 |
CODEN: | ANBCA |
CAS: | peptidase, 9013-14-3, 9031-96-3; trypsin, 9002-07-7; Adenosine Triphosphate, 56-65-5; Peptide Hydrolases, EC 3.4; Phosphorus Radioisotopes; Trypsin Inhibitors; Trypsin, EC 3.4.21.4 |
Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032697_v179_n1_p56_Murray |