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Updated: Aug 16, 2026

Detection of Protein Ubiquitination
Published on: August 19, 2009
Purified uteroglobin lacks anti-proteinase activity
M S López de Haro1, M Pérez Martínez, A Nieto
1Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Cantoblanco, Madrid, Spain.
Abstract:
Rabbit uteroglobin was purified from both uterine fluids and lung lavages by a combination of gel filtration and ion-exchange column chromatography. Anti-trypsin and anti-papain activities were measured in the fractions of the eluates. Anti-proteinase activities were detected in minor contaminants eluting close to the uteroglobin peak but the protein itself was devoid of anti-proteinase activity. Ion-exchange-purified uteroglobin also lacked inhibitory activity of elastase, chymotrypsin or subtilisin. The presence of contaminants could explain the anti-proteinase activity reported occasionally for uteroglobin.
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