Adenylate cyclase and cyclic AMP phosphodiesterase activity during the mitotic cycle of Physarum polycephalum.

Tyrosine, as well as small amounts of phenylalanine, were removed selectively and quantitatively from purified chick brain tubulin by enzymatic digestion with carboxypeptidase. The fraction of molecules containing hydrolyzable tyrosine changed with the stage of development and had the highest value (～0.5) around days 14–16 of the embryo. The increase in the fraction of tyrosinated molecules was found to be temporally correlated with an increased specific activity of the enzyme catalyzing the incorporation reaction. In addition, it was found that the availability of α-chain C-termini for $\text{in vitro}$ tyrosination also reached a maximum during the same period. Changes in the extent of modification of the C-terminus of tubulin may be relevant for the participation of the resultant microbubules in different developmental events.