The procedure for the purification of a basic protein has been reported. Its homogeneity has been established by ultracentrifugation, starch gel electrophoresis, polyacrylamide gel electrophoresis, and end group analysis. Peptide maps of complete tryptic hydrolysates indicate that the molecular weight of this basic protein is 27,000. By immunohistological techniques, it was shown that fluorescent antibody, prepared against the basic protein, reacted specifically with the nuclei of neurons and spermatogonia and did not react with the cell populations in kidney, liver, ovary, and spleen of the same animal. An identical tissue specificity was observed in a variety of animals from tadpole to monkey.
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Tomasi et al. (1968) studied this question.
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