A crosslinked tetrameric alpha 2M that binds but incompletely entraps trypsin.
A crosslinked preparation of alpha-2-macroglobulin was obtained by treatment of the purified human plasma inhibitor with glutaraldehyde at low temperature. The preparation migrated as a 780 KDa polypeptide in SDS-PAGE and with mobility comparable with that of trypsinized native alpha-2-macroglobulin under nondenaturing conditions. Trypsinization of the glutaraldehyde treated alpha-2-macroglobulin further increased its electrophoretic mobility in non-denaturing gels and resulted in the association of the proteinase with the crosslinked inhibitor. Trypsin associated with crosslinked alpha-2-macroglobulin, unlike that associated with native inhibitor was incompletely protected from soybean trypsin inhibition.
Khan
F H
FH
Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, India.
Mirza
M
M
Saleemuddin
M
M
D004591:Electrophoresis, Polyacrylamide Gel; D005976:Glutaral / Q000494:pharmacology*; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D014357:Trypsin / Q000737:chemistry* / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000494:pharmacology; D000511:alpha-Macroglobulins / Q000737:chemistry* / Q000187:drug effects / Q000378:metabolism
D046911:Macromolecular Substances; D014361:Trypsin Inhibitors; D000511:alpha-Macroglobulins; D014357:Trypsin; D005976:Glutaral