Purified uteroglobin lacks anti-proteinase activity.
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.
López de Haro
M S
MS
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Cantoblanco, Madrid, Spain.
Pérez Martínez
M
M
Nieto
A
A
D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008168:Lung / Q000737:chemistry; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000302:isolation & purification*; D011817:Rabbits; D011863:Radioimmunoassay; D014598:Uteroglobin / Q000302:isolation & purification / Q000502:physiology*; D014599:Uterus / Q000737:chemistry
D011480:Protease Inhibitors; D014598:Uteroglobin