Structural changes in alpha-2- and ovomacroglobulins studied by gel chromatography and electron microscopy.
The structural change that occurs in alpha-2-macroglobulin upon its interaction with methylamine or chymotrypsin was studied by high-performance gel chromatography and electron microscopy. The result enabled us to estimate the Stokes radius of the protein as 8.8 nm and 7.9 nm before and after binding with the proteinase, respectively. The methylamine-treated protein also had the Stokes radius of 7.9 nm. Similar studies on the chicken and crocodilian ovomacroglobulins showed that these homologues of alpha 2-macroglobulin had Stokes radii of 9.2-9.3 nm and 8.5-8.7 nm before and after binding with chymotrypsin. Their Stokes radii did not change as a result of the methylamine treatment. Electron micrographs of the native and altered forms of the three proteins are presented. This study introduces a simple and quantitative method to study the structural change of alpha 2-macroglobulin and its homologues.
Nishigai
M
M
Osada
T
T
Ikai
A
A
D000489:Alligators and Crocodiles; D000818:Animals; D002645:Chickens; D002850:Chromatography, Gel / Q000379:methods; D002918:Chymotrypsin; D005260:Female; D006801:Humans; D008259:Macroglobulins / Q000032:analysis*; D008297:Male; D008744:Methylamines; D008854:Microscopy, Electron; D011487:Protein Conformation; D000511:alpha-Macroglobulins / Q000032:analysis*
D008259:Macroglobulins; D008744:Methylamines; D000511:alpha-Macroglobulins; C036828:ovomacroglobulin; C027451:methylamine; D002918:Chymotrypsin