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Differential effects of ubiquitin aldehyde on ubiquitin and ATP-dependent protein degradation.
Biochemistry
August 1996
Department of Biochemistry, University of Iowa College of Medicine, Iowa City 52242-1109, USA.
ATP-dependent proteolysis of 125I-labeled human alpha-globin, bovine alpha-lactalbumin, bovine serum albumin, or chicken lysozyme was assessed in a rabbit reticulocyte extract supplemented with ATP, excess ubiquitin, and variable amounts of ubiquitin aldehyde (Ubal), an inhibitor of many ubiquitin-protein isopeptidases. Low concentrations (0.8 microM) of Ubal increased the ATP-dependent degradation of 125I-alpha-globin by approximately 30% after 2 h at 37 degrees C, had little effect on 125I-lysozyme turnover, and decreased 125I-alpha-lactalbumin or 125I-albumin degradation by approximately 20%.
View Article and Find Full Text PDFFurther studies on immunoglobulin G- and albumin-binding properties of streptococci of serological group L.
Zentralbl Veterinarmed B
September 1995
Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität Giessen, Germany.
In this study, all 88 streptococci of serological group L isolated from cows, pigs, poultry and humans bound 125I-immunoglobulin G, and, in addition, 22 cultures interacted with 125I-albumin. IgG- and albumin-binding sites were solubilized from the streptococcal surface by heat extraction at an acid pH and also by mutanolysin treatment of the bacteria. Western blot analysis of these binding proteins revealed that almost identical protein bands were responsible for 125I-IgG and -albumin binding.
View Article and Find Full Text PDF[Measurement of myeloperoxidase and thiobarbituric acid-reactive material in plasma and bronchoalveolar lavage in E. coli-induced acute lung injury].
Nihon Kyobu Shikkan Gakkai Zasshi
August 1993
Department of Medicine, School of Medicine, Keio University, Tokyo, Japan.
Myeloperoxidase (MPO), which is exclusively contained in neutrophils, is released on their activation. Therefore, MPO may possibly be used as a parameter of neutrophil activation. Thiobarbituric acid-reactive material (TBARM) reflects lipid peroxidation and is a parameter of oxygen radical-mediated cell membrane damage.
View Article and Find Full Text PDFThe albumin receptor effect may be due to a surface-induced conformational change in albumin.
J Biol Chem
June 1989
Medical Research Institute, Mary Imogene Bassett Hospital, Cooperstown, New York 13326.
To determine whether equilibrium binding between albumin and hepatocytes involves a cell surface receptor for albumin, we incubated freshly isolated rat hepatocytes with 125I-albumin and determined the amount of albumin associated with the cells as a function of the total albumin concentration. The resulting two-phase binding curve showed the rat albumin-hepatocyte interaction to consist of a saturable binding interaction with a dissociation constant of 1.1 microM and 2 X 10(6) sites/cell in addition to a weak, nonsaturable binding interaction.
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