Preobrazhenskiĭ A A, Podionova A I, Kasumova S Iu
Biokhimiia. 1988 Nov;53(11):1850-7.
An antigen immunologically related to chordin was identified in white and gray matter of large hemispheres of human brain as well as in one of glial tumours. It was shown that human and rabbit brain extract components cross-react with eight monoclonal antibodies directed against chordin-specific epitopes of P-group. Exhaustive proteolysis of giant sturgeon notochord and human brain extracts resulted in fragments interacting with anti-chordin antibodies and eluted in an equal volume during chromatography on TSK HW-40 gel. At the same time, gel electrophoresis performed under denaturing conditions revealed that the mobility of chordin subunits strikingly differs from that of brain antigen immunologically related to chordin. Thus, the cross-reactivity of antichordin antibodies with the human brain extract component is due to the presence in this antigen of a P-type determinant which, after exhaustive proteolysis of both antigens, is detected in structures (presumably, glycopeptides) having an identical molecular mass.