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Factors influencing the polymerization of outer fibre microtubule protein*

Published online by Cambridge University Press:  17 March 2009

R. E. Stephens
R. E. Stephens
Affiliation:
Department of Biology, Brandies University, Waltham, Massachusetts, U.S.A.
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Extract

Microtubule proteins have recently been prepared and characterized from a number of diverse sources. Renaud, Rowe & Gibbons (1966, 1968) have obtained a protein from acetone powders of Tetrahymena pyriformis cilia and from isolated outer fibre doublets of this same species. The protein has an actin-like amino acid composition, a minimum subunit weight of 55000, and 7·5 free sulphydryl groups per mole of monomer. Stephens (1968a) has fractionated sea-urchin flagella, following the procedure of Gibbons (1965), to obtain the isolated outer fibres and has found the protein to have properties virtually identical to those of its ciliary counterpart. Both the flagellar and the ciliary outer-fibre proteins contain 1 mole of bound guanine nucleotide per mole of protein subunit (Stephens, Renaud & Gibbons, 1967).

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 1 , Issue 4 , January 1969 , pp. 377 - 390
Copyright
Copyright © Cambridge University Press 1969

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References

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