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, 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.
Fernández Murray
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Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina.
Silberstein
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Cantore
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Passeron
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D000255:Adenosine Triphosphate / Q000032:analysis; D000595:Amino Acid Sequence; D001203:Ascomycota / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D014357:Trypsin / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000494:pharmacology
D010761:Phosphorus Radioisotopes; D014361:Trypsin Inhibitors; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases; D014357:Trypsin