Purification and characterization of a mouse mast cell esteroprotease

Yataka Katayama, Joseph V. Auditore, Norman Ende

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


An attempt has been made to isolate, purify, and study the properties of the esteroprotease obtained from neoplastic mouse mast cells. This study revcals that the esteroprotease can be disassociated by DEAE-cellulose chromatography into esterase and protease subunits. However, there is some evidence that suggests that this might represent a macromolecule. Various studies are presented on the esterase and protease subunits as to purification, kinetics, stability, substrate specificity, influence of H ion, Ca ion ion, and inhibitors. The enzyme was found to differ significantly from mouse trypsin and also differs from the trypsin-like enzyme reported in dog and human mast cell. In addition, the esteroprotease enzyme was found to lyse human fibrin and hydrolyze protein in human pleural effusion fluids.

Original languageEnglish (US)
Pages (from-to)228-242
Number of pages15
JournalExperimental and Molecular Pathology
Issue number2
StatePublished - Apr 1971
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Pathology and Forensic Medicine
  • Molecular Biology
  • Clinical Biochemistry


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