| Literature DB >> 7060567 |
Abstract
A high-molecular-weight microtubule-associated protein from chick brain, which has previously been shown to be phosphorylated in vitro to the extent of 10-12 mol X mol-1, is shown to have the same properties as reported for the microtubule-associated protein MAP2 from calf and porcine brain in terms of its molecular weight, sensitivity to trypsin and alpha-chymotrypsin, the molecular weights of the primary proteolytic degradation products, and the failure of certain of the latter components to bind to assembled microtubules. The primary 260,000-Mr tryptic product can be phosphorylated to at least 4 mol X mol-1, in contrast to an earlier report with calf brain MAP2 which noted a single phosphorylation.Entities:
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Year: 1982 PMID: 7060567 DOI: 10.1111/j.1432-1033.1982.tb05843.x
Source DB: PubMed Journal: Eur J Biochem ISSN: 0014-2956