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Effects of S‐100 Proteins on Assembly of Brain Microtubule Proteins: Correlation Between Kinetic and Ultrastructural Data
Author(s) -
Donato Rosario,
Battaglia Francesco,
Cocchia Domenico
Publication year - 1986
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1986.tb04508.x
Subject(s) - microtubule , microtubule nucleation , tubulin , nucleation , in vitro , microbiology and biotechnology , ultrastructure , biophysics , chemistry , elongation , biology , microtubule associated protein , biochemistry , anatomy , cell , materials science , organic chemistry , ultimate tensile strength , cell cycle , centrosome , metallurgy
Microtubules formed in vitro in the presence of S‐100 proteins and micromolar Ca 2+ concentrations are fewer in number and longer than those formed in the presence of Ca 2+ alone. Moreover, microtubules growing after addition of microtubule fragments to a microtubule protein solution in the presence of S‐100 are shorter than those growing in its absence. These data lend support to previous results of kinetic studies indicating that S‐100 interferes with both the nucleation and the elongation of microtubules in vitro.