Developmental alterations in molecular weights of proteins in the human central nervous system that react with antibodies against myelin-associated glycoprotein.

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Abstract
Rat IgG monoclonal antibody (mab), a mouse mab and human serum containing an IgM mab react with isolated human myelin-associated glycoprotien (MAG) on immunoblots and bind only to proteins with relative mobilities identical to MAG and dMAG on immunoblots of homogenates of adult human spinal cord. In homogenates of CNS tissue from human fetuses of gestational ages that antedate myelination, the anti-MAG antibodies react only with proteins with MW of 250,000 or larger. During myelination the MW of proteins with which the anti-MAG antibodies react shift towards the lower MW found in adult myelin. Among those CNS regions examined, the shift towards the low MW occurred earliest in the region that is first to become myelinated and latest in the one that is the last to myelinate. Once myelination is completed, the antibodies react only with proteins with relative mobilities identical to those of MAG and dMAG. These developmental changes in MW of "MAG-related proteins" may prove useful as an index of chemical processes on the basis of which myelination occurs.