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At least 865 records · Page 48Linked to original sources
PubMed1990

An experimental study of the moderator assembly for a low-energy proton accelerator neutron irradiation facility for BNCT.

An accelerator-based neutron irradiation facility (ANIF), which has been proposed for BNCT, is based on a 2.5-MeV proton beam bombarding a thick lithium target. Neutrons which are emitted from the lithium target are too energetic for BNCT and must be moderated. A calculational study, which was done previously on the moderator assembly for an ANIF, shows that, with an optimized moderator assembly, an ANIF can produce a neutron flux which has quality and intensity sufficient for BNCT. In order to verify our previous calculational study, a lithium target and a non-optimized moderator assembly (a cylindrical tank of D2O) have been constructed and tested at the Ohio State University Van de Graaff proton accelerator. The neutron spectrum was measured for neutrons emerging from the moderator assembly. The measured neutron spectrum agrees reasonably well with that obtained from Monte Carlo calculations, except for neutrons with energies above 100 keV. For those neutrons, the measured spectrum is lower by a factor of two than the calculated one. In addition to the neutron spectrum measurement, the boron-10 absorbed dose was measured on the axis of the neutron field in a 20 cm x 20 cm x 20 cm water phantom, and the result agrees quite well with that obtained from calculation. This experiment confirms that the calculated optimized moderator assembly, consisting of a 22.5-cm thick, 25-cm diameter cylinder of beryllia (BeO) surrounded by a 30-cm thick jacket of alumina (Al2O3), produces an epithermal neutron flux of 3.12 x 10(7) n/cm2-s per mA of protons. For an accelerator delivering 30 mA of 2.5-MeV protons, the irradiation time for a single-session treatment can be as short as 50 minutes. The calculated ratio of absorbed neutron dose to fluence for the optimized moderator assembly is 4.9 x 10(-11) cGy-cm2/n, which is equal to that of a 5-keV neutron beam. Our experimental measurements indicate that the ratio of absorbed neutron dose to fluence may in fact be lower (better) than calculated.

Boron↗
PubMed1996

Neuronal assembly dynamics in the rat auditory cortex during reorganization induced by intracortical microstimulation.

Single neurons, acting alone, cannot account for the complex and rapid computations that are routinely accomplished by the behaving nervous system. Recent studies with separable multineuron recordings are showing that neuronal assemblies can indeed be detected and that their organization is very dynamic, depending on variables such as time, physical stimulus, and context. Here we explore both single-neuron and assembly properties in the rat's auditory cortex. Acoustic stimuli are used as a normal, physiological input, and weak electrical intracortical microstimulation (ICMS) as a perturbation that forces a rapid cortical reorganization. In this setting, various aspects of neuronal interactions are changed by the ICMS. We found that cortical neurons exhibited highly synchronous oscillatory firing patterns that were enhanced by ICMS. Cross-correlation studies between two spike trains showed that statistically significant correlations depended on the anatomical distance between the two neurons. ICMS changed the strength and the local number of such correlations. Joint petristimulus analysis and gravity analysis showed that the correlation between neuronal activities varied dynamically at several time scales. We have identified neuronal assemblies in two ways, defined through similarity of receptive field properties and defined through correlated firing. Close anatomical spacing between neurons was conducive to, but not sufficient for membership in, the same assembly with either definition. ICMS changed cortical organization by altering assembly membership. Our data show that neuronal assemblies in the rat auditory cortex can be established transiently in time and that their membership is dynamic.

Acoustic Stimulation↗
PubMed1989

DNA superhelicity enhances the assembly of transcriptionally active chromatin in vitro.

Using an in vitro chromatin assembly system, we analyzed the influence of DNA superhelicity on the development of transcriptionally active minichromosomes. Plasmid DNA molecules containing either a Xenopus borealis 5S RNA gene or an X. laevis methionine tRNA gene were utilized as templates for the assembly of chromatin. Both plasmids were processed into active minichromosomes if introduced as supercoiled molecules into the extract (S-150). The degree of superhelicity is a determining factor in the assembly of active chromatin. Molecules containing varying superhelical densities were processed into minichromosomes with different transcriptional activities. The absence of supercoils leads to the assembly of chromatin with substantially lower transcriptional activity. Assembled minichromosomes are stable enough to be isolated by sucrose gradient centrifugation while retaining their transcriptional phenotype. The formation of nucleosomes with a periodic spacing occurred with the same efficiency and to the same degree regardless of the initial DNA topology. Hence, a determining factor in the development of transcriptionally active chromatin may be the initial superhelicity of the DNA molecule to which activator (trans-acting factors) or repressor (histones) proteins bind. Once the chromatin assembly process has begun, the transcriptional activity of the resulting minichromosome may already have been determined.

Animals↗
PubMed1995

Erythromycin inhibits the assembly of the large ribosomal subunit in growing Escherichia coli cells.

Erythromycin and other macrolide antibiotics have been examined for their effects on ribosome assembly in growing Escherichia coli cells. Formation of the 50S ribosomal subunit was specifically inhibited by erythromycin and azithromycin. Other related compounds tested, including oleandomycin, clarithromycin, spiramycin, and virginiamycin M1, did not influence assembly. Erythromycin did not promote the breakdown of ribosomes formed in the absence of the drug. Two erythromycin-resistant mutants with alterations in ribosomal proteins L4 and L22 were also examined for an effect on assembly. Subunit assembly was affected in the mutant containing the L22 alteration only at erythromycin concentrations fourfold greater than those needed to stop assembly in wild-type cells. Ribosomal subunit assembly was only marginally affected at the highest drug concentration tested in the cells that contained the altered L4 protein. These novel results indicate that erythromycin has two effects on translation, preventing elongation of the polypeptide chain and also inhibiting the formation of the large ribosomal subunit.

Anti-Bacterial Agents↗
PubMed1988

Brush border myosin filament assembly and interaction with actin investigated with monoclonal antibodies.

Monoclonal antibodies binding to epitopes in the rod portion of brush border myosin were used to study the mechanism of filament assembly and its role in myosin interaction with actin. The antibodies and their Fab fragments had specific effects on the size of the filaments assembled in vitro. Two antibodies (BM3 and BM4), directed against the tip of the myosin tail, completely inhibited myosin filament assembly. The other antibodies (BM1, BM2 and BM5), binding to other sites along the myosin rod, only partially blocked filament growth, and short filaments could be assembled. Thiophosphorylated brush border myosin filaments appeared slightly more stable to the effects of the antibodies than those composed of dephosphorylated myosin. Only one (BM3) of the antibodies which completely inhibited the assembly of new filaments was capable of disassembling preformed myosin filaments. The other antibody, BM4, partially disassembled filaments, leaving approximately 0.2-microns long 'cores', suggesting that polymerization in this myosin occurs by a biphasic mechanism, i.e. the formation of a stable nucleus of antiparallely packed molecules, followed by elongation. The antibodies BM1 and BM2 bound to myosin filaments generating a regular transverse pattern with a approximately 14-nm periodicity, and had little effect on the stability of these preformed filaments. Inhibition of filament formation and solubilization of the myosin by the antibodies appeared to be associated with inhibition of myosin interaction with actin, as measured by the actin-activated MgATPase activity. In the presence of the antibodies which completely inhibit filament assembly, we observed a decrease to approximately 20% (BM4-Fab) and to approximately 50% (BM3) of the control actin-activated myosin MgATPase activity, and this activity was kinetically different from that of the soluble myosin S1 fragment, suggesting that the rod has a profound effect on the kinetics of actomyosin interaction.

Actins↗
PubMed2001

Three-dimensional and fractal analyses of assemblies of amyloid beta protein subtypes [Abeta40 and Abeta42(43)] in canine senile plaques.

The three-dimensional (3D) distribution of amyloid beta protein (Abeta) subtypes [Abeta40 and Abeta42(43)] in canine senile plaques (SP) was observed using a confocal laser scanning microscope. In diffuse plaques (DP), Abeta42(43) alone was deposited as an uneven nebula-like assembly of fine granules. The border of the Abeta42(43) assembly was unclear and diffusely merged to the surrounding area. Mature plaques (MP), on the other hand, showed two patterns of Abeta deposition. In some MP, only Abeta40 was deposited as a defined assembly of very short fibrillary structures. Other MP consisted of both Abeta40 and Abeta42(43), and the deposition patterns of the two Abeta species were the same as those in single-positive plaques; fine granular with unclear margin for Abeta42(43), and short fibrillary structures for Abeta40. Additionally, we calculated the fractal dimensions (FD) of both Abeta40 and Abeta42(43) assemblies, and examined the serial change of FD in each SP. The FD of Abeta42(43)-positive DP ranged from 1.05 to 1.27, and those of Abeta40-positive MP ranged from 1.13 to 1.54 in single-positive plaques. In one double-positive MP, FD ranged from 1.02 to 1.36 for Abeta42(43) and from 1.01 to 1.51 for Abeta40. These results showed that the FD of canine Abeta40 assemblies was higher than that of Abeta42(43) assemblies, and the spatial changes of FD values for Abeta40 and Abeta42(43) in double-positive plaques were quite different. These morphological analyses clearly showed that canine DP and MP have completely different 3D structures, suggesting that their processes of formation are different.

Alzheimer Disease↗
PubMed1996

Neural assemblies and laminar interactions in the cerebral cortex.

Neural assemblies are assumed to become organized and to operate within the cerebral cortex, and so must be constrained by the cytological and physiological properties of this laminated structure. A hypothesis of such assemblies is presented, based on important details of neuronal architecture and physiology in different cortical laminae. Laminae II, III and VI, which are the origin and termination of most cortico-cortical projections, are regarded as the site of storage of most of the information encoded by assemblies - a neuronal 'library'. Laminae II and III are the most sensitive coincidence detectors, and therefore probably initiate the process of assembly formation. However, these three laminae have very low levels of spontaneous activity in the waking state, and so active cell assemblies cannot base their functioning on these laminae alone. Lamina V pyramidal cells have a much higher level of spontaneous activity. Thus, indirect pathways between 'library' cells, via lamina V pyramidal cells, are likely to be more secure than direct ones. It is proposed that direct links between 'library' cells become stabilized by Hebbian strengthening, once the recipient 'library' cell has been 'primed' by neural activity transmitted indirectly via lamina V neurones. Thus lamina V neurones could catalyse the process of assembly formation. Given this proposal, lamina V cells, in their interaction with 'library' cells, would code information in terms of precisely timed individual impulses, but would employ a code based on slower frequency changes in their descending influences upon neural centres in the brainstem and spinal cord. Predictions for single unit and electrographic experiments are discussed.

Afferent Pathways↗
PubMed2001

Abortive assembly of succinate-ubiquinone reductase (complex II) in a ferrochelatase-deficient mutant of Escherichia coli.

Heme molecules play important roles in electron transfer by redox proteins such as cytochromes. In addition, a structural role for heme in protein folding and the assembly of enzymes has been suggested. Previous results obtained using Escherichia coli hemA mutants, which are unable to synthesize 5-aminolevulinic acid, a precursor of porphyrins and hemes, have demonstrated a requirement for heme biosynthesis in the assembly of a functional succinate-ubiquinone reductase (SQR or complex II), which is a component of the aerobic respiratory chain. In the present study, in order to investigate the role of the heme in the assembly of E. coli SQR, we used a hemH (encodes ferrochelatase) mutant that lacks the ability to insert iron into the porphyrin ring. The hemH mutant failed to insert functional SQR into the cytoplasmic membrane, and the catalytic portion of SQR [the flavoprotein subunit (Fp) and the iron-sulfur protein subunit (Ip)] was localized in the cytoplasm of the cell. It is of interest to note that protoporphyrin IX accumulated in the mutant cells and inactivated the cytoplasmic succinate dehydrogenase (SDH) activity associated with the catalytic Fp-Ip complex. In contrast, SQR was assembled into the membrane of a heme-permeable hemH double mutant when hemin was present in the culture. Only a low level of SQR activity was found in the membrane when hemin was replaced by non-iron metalloporphyrins: Mn-, Co-, Ni-, Zn- and Cu-protoporphyrin IX, or protoporphyrin IX These results indicate that heme iron is indispensable for the functional assembly of SQR in the cytoplasmic membrane of E. coli, and provide a new insight into the biological role of heme in the molecular assembly of the multi-subunit enzyme complex.

Cell Membrane↗
PubMed1996

Ergonomics in parallelized car assembly: a case study, with reference also to productivity aspects.

In 1985 Volvo started the development of a new plant for the assembling of cars. This plant was situated in the town of Uddevalla in Sweden. One deliberate aim with this plant was to combine an enhanced productivity and product quality with good ergonomics conditions and improved work organization. The plant was designed with a production system where parallel work-teams of about five persons could assemble from 1/4 up to complete cars. A newly developed tilting device, a piece of equipment that could rotate, rise and lower the car body in order to facilitate assembly work, was introduced. Ergonomic analyses of postural and musculoskeletal strain showed that parallelized flow production, according to the production principles of the Uddevalla plant, was superior to traditional car assembly according to the serial flow production concept, i.e. the traditional assembly line. It was noted that this ergonomic standard was implemented without compromising productivity. In conclusion, increased knowledge and experience of parallelized production systems has been gained which should be considered in the development of future assembly plants, even though the Uddevalla factory itself was closed down in 1993.

Journal Article↗
PubMed1987

Effect of estramustine phosphate on the assembly of trypsin-treated microtubules and microtubules reconstituted from purified tubulin with either tau, MAP2, or the tubulin-binding fragment of MAP2.

Estramustine phosphate, an estradiol nitrogen-mustard derivative is a microtubule-associated protein (MAP)-binding microtubule inhibitor, used in the therapy of prostatic carcinoma. It was found to inhibit assembly and to induce disassembly of microtubules reconstituted from phosphocellulose-purified tubulin with either tau, microtubule-associated protein 2, or chymotrypsin-digested microtubule-associated protein 2. Estramustine phosphate also inhibited assembly of trypsin-treated microtubules, completely depleted of high-molecular-weight microtubule-associated proteins, but with their microtubule-binding fragment present. In all cases estramustine phosphate induced disassembly to about 50%, at a concentration of approximately 100 microM, at similar protein concentrations. However, estramustine phosphate did not affect dimethyl sulfoxide-induced assembly of phosphocellulose-purified tubulin. Estramustine phosphate is a reversible inhibitor, as the nonionic detergent Triton X-100 was found to counteract the inhibition in a concentration-dependent manner. The reversibility was nondisruptive, as Triton X-100 itself did not affect microtubule assembly, microtubule protein composition, or morphology. This new reversible MAPs-dependent inhibitor estramustine phosphate affects the tubulin assembly, induced by tau, as well as by the small tubulin-binding part of MAP2 with the same concentration dependency. This indicates that tau and the tubulin-binding part of MAP2, in addition to their assembly promoting functions also have binding site(s) for estramustine phosphate in common.

Binding Sites↗
PubMed1993

Each of three positively-charged amino acids in the C-terminal region of yeast mitochondrial ATP synthase subunit 8 is required for assembly.

Each of three conserved positively-charged residues in the C-terminal region of subunit 8 of yeast (Saccharomyces cerevisiae) mitochondrial ATP synthase was replaced with isoleucine. The assembly and functional properties of the resulting variants (substituted at Arg-37, Arg-42 and Lys-47) were examined using in-vitro systems to assay import into isolated mitochondria and to monitor assembly into ATP synthase, as well as an in-vivo rescue system using host yeast cells lacking endogenous subunit 8. Each such variant was found to be impaired in assembly in vitro, after import in the form of a chimaeric protein bearing a leader sequence with mitochondrial targeting function. Import precursors bearing a duplicated-leader sequence, engendering enhanced delivery to mitochondria of the passenger variant subunit-8 proteins, enabled assembly of the (Lys-47-->Ile) variant to be detected in vitro but not that of (Arg-37-->Ile) or (Arg-42-->Ile) variants. The respiratory growth of subunit 8-deficient host cells could be rescued with the (Lys-47-->Ile) variant expressed allotopically in the nucleus. Such rescued cells were found to have an enhanced growth rate (comparable to that produced by non-mutagenized parental subunit 8) when delivered to mitochondria with the duplicated-leader sequence, as compared to the single-leader sequence. This confirms that the impediment in the (Lys-47-->Ile) variant lies in the efficiency of its assembly, rather than a functional defect, as such, arising from the loss of that positive charge. In contrast, host cells were unable to be rescued by the (Arg-37-->Ile) and (Arg-42-->Ile) variants, even when they were endowed with the duplicated leader sequence. It is concluded that the positively-charged C-terminal domain of subunit 8, common to fungal and mammalian homologues of this protein, plays a key role in its assembly into mitochondrial ATP synthase.

Base Sequence↗
PubMed1984

Mechanism of action of S-100 protein(s) on brain microtubule protein assembly.

The inhibitory effect of S-100 on microtubule protein assembly is inversely related to the microtubule protein concentration and/or the temperature of assembly. Moreover, the S-100-induced decrease in the rate and extent of assembly is positively correlated with the length of the lag of assembly. When microtubule fragments are added to the microtubule protein solution, the S-100 effect is reduced but not abolished. These data suggest that S-100 interferes with both the nucleation and the elongation of microtubules. Since S-100 also inhibits the assembly of purified tubulin, S-100 is suggested to affect the microtubule assembly by interacting with and sequestering tubulin.

Animals↗
PubMed1986

Evidence that S100 proteins regulate microtubule assembly and stability in rat brain extracts.

Microtubule re-assembly in rat brain extracts was inhibited by antibodies to S100 proteins. Anti-S100 antibodies caused an increase in the cold-stability of microtubules and this effect was abolished by the presence of short lengths of microtubules formed under control conditions. Anti-S100 antibodies had no effect on the stimulation of assembly or the increase in microtubule stability caused by low zinc concentrations. Addition of exogenous S100a and S100b to brain extracts had different effects on assembly; S100a caused an inhibition of assembly while S100b stimulated the early phase of assembly. The data suggest that endogenous S100b is involved in the regulation of microtubule assembly in brain extracts.

Animals↗
PubMed1986

Assembly and disassembly of bacteriophage T4 polyheads.

The assembly of the product of bacteriophage T4 gene 23 (gp23), the uncleaved form of the main shell protein, has been studied. Assembly and disassembly follow the predictions for entropy-driven processes; assembly is strongly favored by conditions of high salt concentrations and high temperatures, whereas low salt and low temperatures promote disassembly. In the absence of the scaffolding core proteins in vitro, only polyheads, the tubular variant of the prohead, are produced. Kinetic studies show that the rate of polyhead dissociation depends on the concentration of associated protein, not on the number and length of the particles. Comparable to crystal formation, assembly of gp23 occurs above a critical concentration, which is dependent on salt concentration, pH and temperature. These characteristics are common to most self-assembling systems. The oligomeric states of gp23 have been investigated by analytical ultracentrifugation, which indicated the existence, at very low salt concentration and low temperature, of an equilibrium between monomers and higher oligomers, culminating in the hexamer. At pH 9.0 polyheads are completely dissociated into their monomeric gp23 subunits. Our data suggest that the hexamer is a true intermediate of polyhead assembly.

Escherichia coli↗
PubMed1988

Roles of operator and non-operator RNA sequences in bacteriophage R17 capsid assembly.

In order to understand the role of sequences other than the translational operator on bacteriophage R17 assembly, in vitro capsid assembly was studied with R17 coat protein and a variety of RNAs. For a series of RNA oligomers of the same chain length, sequences that bind coat protein dimer with a lower affinity require higher concentrations of RNA and protein for assembly. Among a series of non-specific RNA molecules of differing lengths, lower protein and RNA concentrations are required for assembly of capsids containing longer RNAs. For RNA molecules of any length, the presence of a single high-affinity translational operator sequence lowered the concentration requirements for capsid assembly. However, the advantage for encapsidation provided by the operator sequence is small for large RNA molecules. The experiments indicate that in the overall assembly process the interaction of coat protein with non-specific sequences is at least as important as its interaction with the specific translational operator sequence. In light of the data, a mechanism of achieving selective packaging of the R17 genomic RNA in vivo is discussed.

Bacteriophages↗
PubMed1989

Assembly and properties of chromatin containing histone H1.

The Xenopus oocyte supernatant (oocyte S-150) forms chromatin in a reaction that is affected by temperature and by the concentration of ATP and Mg. Under optimal conditions at 27 degrees C, relaxed DNA plasmids are efficiently assembled into supercoiled minichromosomes with the endogenous histones H3, H4, H2A and H2B. This assembly reaction is a gradual process that takes four to six hours for completion. Micrococcal nuclease digestions of the chromatin assembled under these conditions generate an extended series of DNA fragments that are, on average, multiples of 180 base-pairs. We have examined the effect of histone H1 in this system. Exogenous histone H1, when added at a molar ratio of H1 to nucleosome of 1:1 to 5:1, causes an increase in the micrococcal nuclease resistance of the chromatin without causing chromatin aggregation under these experimental conditions. Furthermore, the periodically arranged nucleosomes display longer internucleosome distances, and the average length of the nucleosome repeat is a function of the amount of histone H1 added, when this histone is present at the onset of the assembly process. In contrast, no major change in the length of the nucleosome repeat is observed when histone H1 is added at the end of the chromatin assembly process. Protein analyses of the purified minichromosomes show that histone H1 is incorporated in the chromatin that is assembled in the S-150 supplemented with histone H1. The amount of histone H1 bound to chromatin is a function of the total amount of histone H1 added. We define here the parameters that generate histone H1-containing chromatin with native nucleosome repeats from 160 to 220 base-pairs, and we discuss the implications of these studies.

Adenosine Triphosphate↗
PubMed1992

Identification of a nonapeptide motif in the vimentin head domain involved in intermediate filament assembly.

The assembly of soluble vimentin subunits into intermediate filaments (IFs) is dependent on information located in the amino-terminal domain. Using site-directed mutagenesis of a Xenopus laevis vimentin cDNA and an Escherichia coli production system to obtain pure mutated protein, we have identified, in the head domain, a nine amino acid motif (SSYRRIFGG), evolutionarily conserved from amphibia to man, which plays an important role in the orderly formation of IFs. Exchanges in the central di-arginine and in the two aromatic residues interfere with IF assembly of vimentin in vitro: on assembly under standard assembly conditions (160 mM-NaCl) most of the protein is included in dense aggregates, with a variable and minor proportion of IFs, whereas at lower ionic concentrations short and incomplete IF-like structures are formed. The deletion of the whole motif results in a protein that under standard assembly conditions (e.g. 160 mM-NaCl) predominantly and rapidly precipitates into large aggregates of non-IF material, whereas at lower ionic strength (e.g. 50 mM-NaCl) both IFs and dense aggregates are formed simultaneously. Our results show that the mutated protein can assume different forms at the same time and under the same conditions. This motif alone is insufficient for the formation of normal IFs as demonstrated by a mutant in which the motif has been brought closer to the alpha-helical rod domain by deletion of 55 internal amino acid residues. Corresponding observations have been made, by immunofluorescence microscopy, upon transfection of cultured epithelial cells lacking vimentin IFs. The importance of the head domain motif for the assembly and higher-order arrangement of IFs is discussed.

3T3 Cells↗
PubMed1988

The in vitro porcine brain tubulin assembly assay: effects of a genotoxic carcinogen (aflatoxin B1), eight tumor promoters and nine miscellaneous substances.

Aflatoxin B1 (AFB1) had a reversible inhibitory effect on the assembly of porcine brain tubulin in vitro. The 30%-inhibition concentration was 0.3 mM AFB1. The 8 tumor promoters showed different effects. Five of them, anthralin, cholic acid, gamma-hexachlorocyclohexane (lindane, gamma-HCH), lithocholic acid and phenobarbital (PB), enhanced the in vitro assembly. The effect was reversible in the case of PB and anthralin, only partially reversible in the case of cholic acid and gamma-HCH, whereas the stimulating effects of lithocholic acid led to an irreversible modification of the tubulin structure, as shown by the insolubility of the microtubules at 0 degrees C. This could be confirmed by an electron microscopic study. The doses necessary for a 30% enhancement of the steady-state level were 3 mM (PB), 0.2 mM (anthralin), 6 mM (cholic acid), 0.7 mM (gamma-HCH) and less than 0.2 mM (lithocholic acid). The other 3 tumor promoters tested - diethylstilbestrol (DES), 4,4'-dichloro-diphenyl-trichloro-ethane (DDT) and saccharin - inhibited the assembly. The concentrations necessary for a 30% inhibition varied within a wide range: 0.025 mM, 0.4 mM and 7.5 mM for DES, DDT and saccharin, respectively. Five of the 9 miscellaneous compounds, namely asbestos (crocidolite), bavistan, colchicine, chloropropham and ethylacetate, showed inhibitory effects, whereas Fe2+ (a constituent of asbestos) and 5-azacytidine did not influence the assembly process. The 30%-inhibition concentrations for colchicine, ethylacetate and asbestos were 10 microM, 0.153 M and 0.19 mM, respectively. For bavistan and chloropropham the 30%-inhibition values were 0.7 mM and 2.0 mM, respectively. The inhibitory effects of chloropropham and asbestos were reversible. For colchicine and bavistan the reversibility of the effects was not assayed. In agreement with published data, dimethylsulfoxide (DMSO) and acetone enhanced the in vitro assembly of porcine brain tubulin. The doses needed for a 30% enhancement by DMSO and acetone were 0.4 mM and 0.136 M, respectively. The effect of DMSO was irreversible whereas acetone led to a reversible stimulation. Some compounds were tested for their influence on preformed microtubules (interaction with the equilibrium between assembly and disassembly). Anthralin, cholic acid, PB and DMSO showed no effect on the steady-state plateau. A slight reduction was induced by DDT and bavistan, whereas DES, colchicine and chloropropham led to a pronounced reduction.

Aflatoxins↗