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- Title
Mannan-Binding Protein Forms Complexes with α-2-Macroglobulin. A Proposed Model for the Interaction.
- Authors
Storgaard, P.; Nielsen, E. Holm; Skriver, E.; Andersen, O.; Svehag, S.-E.
- Abstract
We report that α-2-macroglobulin (α2M) can form complexes with a high molecular weight porcine mannan-binding protein (pMBP-28). The α2M/pMBP-28 complexes were isolated by PEG-precipitation and affinity chromatography on mannan-Sepharose, protein A-Sepharose and anti-IgM Sepharose. The occurrence of α2M/pMBP-28 complexes was further indicated by crossed immunoelectrophoresis and by use of an anti-α2M affinity column and chelating Sepharose loaded with Zn2+. The eluates from these affinity columns showed α2M subunits (94 and 180 kDa) and pMBP subunits (28 kDa) in SDS-PAGE, which reacted with antibodies against α2M and pMBP-28, respectively, in Western blotting. Furthermore, the α2M/pMBP-28 complexes were demonstrated by electron microscopy. Fractionation of pMBP-containing D-mannose eluate from mannan-Sepharose on Superose 6 showed two protein peaks which reacted with anti-Cl s antibodies in ELISA, one of about 650-800 kDa, which in addition contained pMBP-28 and anti-α2material, the other with an Mr of 100-150kDa. The latter peak revealed rhomboid molecules (7 x 15nm) in the electron microscope and a 67 kDa band in SDS-PAGE under reducing conditions. This band was also seen in eluates from the anti-α2M and chelating Sepharose columns. Based on these observations and previous findings by other investigators of a serine protease with about 67 kDa subunits which copurifies with human MBP we propose a model for the interaction of pMBP-28 with α2M.
- Subjects
CARRIER proteins; MACROGLOBULINS; SEPHAROSE; GEL permeation chromatography; ZONE electrophoresis
- Publication
Scandinavian Journal of Immunology, 1995, Vol 42, Issue 3, p373
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1995.tb03670.x