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- W2080620164 abstract "— Incorporation of [14C]tyrosine into the C-terminal position of α-tubulin of rat brain cytosol was 10-fold higher for non-assembled than for assembled tubulin. The incorporation into tubulin from disassembled microtubules was higher than into non-assembled tubulin; therefore, the low incorporation into microtubules was not due to a lower acceptor capacity of their tubulin constituent.[14C]Tyrosine was released from assembled and non-assembled [14C]tyrosinated tubulin by the action of an endogenous carboxypeptidase. Release from non-assembled tubulin was shown by incubating a tubulinyl-[14C]tyrosine preparation in the presence of CaCl2 at a concentration that abolished microtubule formation. Release from microtubules was inferred from the observation that the percentages of [14C]tyrosine released and the decrease of the specific radioactivity of the recovered microtubules were practically identical and did not change after a 10-fold dilution of the incubated microtubules.[3H]Phenylalanine was released from a preparation of tubulinyl-[3H]phenylalanine also by an enzymatic activity.The capacity of a tubulin preparation to incorporate tyrosine was increased 43% by pre-treatment with endogenous carboxypeptidase.Tubulin tyrosinated in vitro was assembled to the same extent as native tubulin. After a mixture of tubulinyl-[14C]tyrosine and tubulinyl-[3H]phenylalanine was partially assembled, the ratio of 14C/3H found in the microtubules was the same as in the non-assembled tubulin fraction." @default.
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- W2080620164 date "1978-07-01" @default.
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- W2080620164 title "CAPABILITY OF TUBULIN AND MICROTUBULES TO INCORPORATE AND TO RELEASE TYROSINE AND PHENYLALANINE AND THE EFFECT OF THE INCORPORATION OF THESE AMINO ACIDS ON TUBULIN ASSEMBLY" @default.
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- W2080620164 doi "https://doi.org/10.1111/j.1471-4159.1978.tb12449.x" @default.
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