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![Research paper thumbnail of Polyribosome Formation in Relation to Cytokinin-induced Cell Division in Suspension Cultures of Glycine max [L.] Merr](https://attachments.academia-assets.com/84775021/thumbnails/1.jpg)
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Plant Molecular Biology Reporter, 1994
This advanced undergraduate textbook examines plant growth and development from a molecular and g... more This advanced undergraduate textbook examines plant growth and development from a molecular and genetic perspective in the following 10 chapters: introduction (to the plant body and the differences between developmental mechanisms in plants and animals); the genetic basis of plant ...
Planta, Feb 1, 1987
The inhibition of the polymerization of tubulin from cultured cells of rose (Rosa. sp. cv. Paul's... more The inhibition of the polymerization of tubulin from cultured cells of rose (Rosa. sp. cv. Paul's scarlet) by colchicine and the binding of colchicine to tubulin were examined in vitro and compared with data obtained in parallel experiments with bovine brain tubulin. Turbidimetric measurements of taxol-induced polymerization of rose microtubules were found to be sensitive and semiquantitative at low tubulin concentrations, and to conform to some of the characteristics of a nucleation and condensation-polymerization mechanism for assembly of filamentous helical polymers. Colchicine inhibited the rapid phase of polymerization at 24 ~ C with an apparent inhibition constant (Ki) of 1.4.10-4 M for rose tubulin and an apparent Ki= 8.8" 10-v M for brain tubulin. The binding of [3H]colchicine to rose tubulin to form tubulin-colchicine complex was mildly temperature-dependent and slow, taking 2-3 h to reach equilibrium at 24 ~ C, and was not affected by vinblastine sulfate. The binding of [3H]colchicine to rose tubulin was saturable and Scatchard analysis indicated a single class of low-affinity binding sites having an apparent affinity constant (K) of 9.7.102 M-1 and an estimated molar binding stoichiometry (r) of 0.47 at 24 ~ C. The values for brain tubulin were K=2.46" 106 M-1 and r=0.45 at 37 ~ C. The binding of [3H]colchicine to rose tubulin was inhibited by excess unlabeled colchicine, but not by podophyllotoxin or tropolone. The data demonstrate divergence of the colchicine-binding sites on plant and animal tubulins and indicate that the relative resistance of plant microtubule polymerization to
Morphogenesis in Plants, 1993
Cell and Molecular Biology of the Cytoskeleton, 1986
Proceedings in Life Sciences, 1980
Advances in Experimental Medicine and Biology, 1972
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Science Letters, 1983
Plant Molecular Biology Reporter, 1994
This advanced undergraduate textbook examines plant growth and development from a molecular and g... more This advanced undergraduate textbook examines plant growth and development from a molecular and genetic perspective in the following 10 chapters: introduction (to the plant body and the differences between developmental mechanisms in plants and animals); the genetic basis of plant ...
Planta, Feb 1, 1987
The inhibition of the polymerization of tubulin from cultured cells of rose (Rosa. sp. cv. Paul's... more The inhibition of the polymerization of tubulin from cultured cells of rose (Rosa. sp. cv. Paul's scarlet) by colchicine and the binding of colchicine to tubulin were examined in vitro and compared with data obtained in parallel experiments with bovine brain tubulin. Turbidimetric measurements of taxol-induced polymerization of rose microtubules were found to be sensitive and semiquantitative at low tubulin concentrations, and to conform to some of the characteristics of a nucleation and condensation-polymerization mechanism for assembly of filamentous helical polymers. Colchicine inhibited the rapid phase of polymerization at 24 ~ C with an apparent inhibition constant (Ki) of 1.4.10-4 M for rose tubulin and an apparent Ki= 8.8" 10-v M for brain tubulin. The binding of [3H]colchicine to rose tubulin to form tubulin-colchicine complex was mildly temperature-dependent and slow, taking 2-3 h to reach equilibrium at 24 ~ C, and was not affected by vinblastine sulfate. The binding of [3H]colchicine to rose tubulin was saturable and Scatchard analysis indicated a single class of low-affinity binding sites having an apparent affinity constant (K) of 9.7.102 M-1 and an estimated molar binding stoichiometry (r) of 0.47 at 24 ~ C. The values for brain tubulin were K=2.46" 106 M-1 and r=0.45 at 37 ~ C. The binding of [3H]colchicine to rose tubulin was inhibited by excess unlabeled colchicine, but not by podophyllotoxin or tropolone. The data demonstrate divergence of the colchicine-binding sites on plant and animal tubulins and indicate that the relative resistance of plant microtubule polymerization to
Morphogenesis in Plants, 1993
Cell and Molecular Biology of the Cytoskeleton, 1986
Proceedings in Life Sciences, 1980
Advances in Experimental Medicine and Biology, 1972
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Growth and Development, 1994
Plant Science Letters, 1983