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pubmed:abstractText |
We have developed a thrombin proteolytic cleavage procedure to obtain higher yields of the Mr 28,000 microtubule-binding and Mr 240,000 microtubule-projection components of MAP-2. The former is a highly basic component, whereas the latter and intact MAP-2 are acidic polypeptides. Most notably, our studies reveal that this Mr 28,000 fragment binds to neurofilaments, but the Mr 240,000 projection domain fails to interact. These data indicate that microtubules and neurofilaments share a common binding site on high-molecular-weight MAP-2.
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