Characterization of albumin-binding properties of Peptostreptococcus magnus.
A Peptostreptococcus magnus strain demonstrated binding activity for albumin preparations from humans, mice, and dogs, but not for rabbit or bovine albumin. The albumin binding site appeared to be heat stable and of protein nature. Treatment of P. magnus cells with trypsin under specified conditions enhanced this albumin binding. Electron micrographs and kinetic analyses revealed that this enhancement was the result of the removal of some cell wall associated proteins leading to a higher binding affinity without significant changes in binding site numbers. The albumin-binding proteins could be readily solubilized and purified by affinity chromatography. Upon gel electrophoresis the molecular mass of the albumin-binding proteins was estimated as 130 kilodaltons.
Institut für Bakteriologie und Immunologie, Justus-Liebig-Universität Giessen, Federal Republic of Germany.
C
C
Lämmler
A
A
Alaboudi
A
A
Hildebrand
D000418:Albumins / Q000378:metabolism*; D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D004285:Dogs; D006801:Humans; D051379:Mice; D010462:Peptostreptococcus / Q000378:metabolism*; D011817:Rabbits; D013045:Species Specificity
D000418:Albumins; D001426:Bacterial Proteins; D002352:Carrier Proteins