Binding of alpha 2-macroglobulin and haptoglobin to Actinomyces pyogenes.
All 25 cultures of Actinomyces pyogenes tested in the present study bound 125I-labelled human alpha 2-macroglobulin with a mean binding of 65.6%. Thirteen cultures also bound 125I-labelled human haptoglobin with a mean of 51.5%. None interacted with fibrinogen, fibronectin, immunoglobulin G, or albumin. Twenty-eight cultures representing other species of actinomycetaceae did not show any interaction with alpha 2-macroglobulin, haptoglobin, and other plasma proteins tested. The binding of alpha 2-macroglobulin and haptoglobin to A. pyogenes was saturable and could be completely inhibited by the respective unlabelled plasma proteins. The binding of alpha 2-macroglobulin could not be inhibited by unlabelled haptoglobin. On the other hand, alpha 2-macroglobulin blocked the binding of haptoglobin, possibly by steric hindrance. Treatment of the bacteria with trypsin reduced their binding activities for alpha 2-macroglobulin and haptoglobin indicating the protein nature of the binding sites. Exposure to heat (1 h, 80 degrees C) significantly diminished the binding activity for haptoglobin, but not that for alpha 2-macroglobulin. The binding of alpha 2-macroglobulin and haptoglobin could be an important feature in the classification of A. pyogenes among the members of actinomycetaceae.
C
C
Lämmler
G S
GS
Chhatwal
H
H
Blobel
D000190:Actinomyces / Q000145:classification / Q000378:metabolism; D001665:Binding Sites / Q000187:drug effects; D003352:Corynebacterium / Q000145:classification / Q000378:metabolism*; D006242:Haptoglobins / Q000378:metabolism*; D006801:Humans; D007457:Iodine Radioisotopes; D011485:Protein Binding; D013045:Species Specificity; D014357:Trypsin / Q000494:pharmacology; D000511:alpha-Macroglobulins / Q000378:metabolism*
D006242:Haptoglobins; D007457:Iodine Radioisotopes; D000511:alpha-Macroglobulins; D014357:Trypsin