Abstract
A high MW, microtubule-associated protein from chick brain, previously shown to be phosphorylated in vitro to the extent of 10-12 mol .cntdot. mol-1, has the same properties as reported for the microtubule-associated protein MAP2 from calf and porcine brain in terms of its MW, sensitivity to trypsin and .alpha.-chymotrypsin, the MW of the primary proteolytic degradation products and the failure of certain of the latter components to bind to assembled microtubules. The primary 260,000-MW tryptic product can be phosphorylated to at least 4 mol .cntdot. mol-1, in contrast to an earlier report with calf brain MAP2 which noted a single phosphorylation site.