Biochemical Journal · 1979 · 28 citations · 19 references
Life SciencesBiochemistryMolecular BiologyEnzyme MechanismEnzymologyProtein BiochemistryEnzyme CharacterizationEnzyme PurificationProteolytic EnzymesDigestive Enzyme PurificationDigestive ProteasesDipeptidyl PeptidasesIntestinal EnzymesPeptidase Activity
Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa, was purified to homogeneity. The pure enzyme is a glycoprotein containing a very small amount of sugar. It is composed of only one subunit of 50,000 mol. wt. and possesses 1 zinc atom per molecule. Its specificity is primarily directed towards tripeptides with an N-terminal proline residue. However, the enzyme is also able to hydrolyse other tripeptides, except those with either a charged amino acid in the N-terminal position or a proline residue in the second position. The purified aminotripeptidase accounts for almost all the tripeptidase activity of the soluble fraction from intestinal mucosa.
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The Thiobarbituric Acid Assay of Sialic Acids
Leonard Warren · Journal of Biological Chemistry · 1959 · 6.4K citations · Full text