TY - JOUR
T1 - Translation in vitro of rat brain messenger RNA coding for tubulin and actin
AU - Gozes, I.
AU - Schmitt, H.
AU - Littauer, U. Z.
PY - 1975
Y1 - 1975
N2 - A partially purified fraction of poly (A) rich brain mRNA coding for tubulin and actin was obtained by stepwise elution from an oligo (deoxythymidylate) cellulose column and was efficiently translated in a wheat germ cell free system. The newly synthesized tubulin and actin migrated along with the authentic proteins on sodium dodecyl sulfate polyacrylamide gels and on sodium dodecyl sulfate urea polyacrylamide gels, where tubulin α and β subunits are separated. The two proteins synthesized in vitro were found to be biologically active; they could be induced to polymerize and were both precipitated by vinblastine. In addition, specific binding of tubulin to an affinity column of colchicine Sepharose and actin to myosin were demonstrated.
AB - A partially purified fraction of poly (A) rich brain mRNA coding for tubulin and actin was obtained by stepwise elution from an oligo (deoxythymidylate) cellulose column and was efficiently translated in a wheat germ cell free system. The newly synthesized tubulin and actin migrated along with the authentic proteins on sodium dodecyl sulfate polyacrylamide gels and on sodium dodecyl sulfate urea polyacrylamide gels, where tubulin α and β subunits are separated. The two proteins synthesized in vitro were found to be biologically active; they could be induced to polymerize and were both precipitated by vinblastine. In addition, specific binding of tubulin to an affinity column of colchicine Sepharose and actin to myosin were demonstrated.
UR - http://www.scopus.com/inward/record.url?scp=0016609219&partnerID=8YFLogxK
U2 - 10.1073/pnas.72.2.701
DO - 10.1073/pnas.72.2.701
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AN - SCOPUS:0016609219
SN - 0027-8424
VL - 72
SP - 701
EP - 705
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 2
ER -