Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0085631 (agitation)
 12,064 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Several tests were devised to further characterize deoxyribonucleic acid (DNA) synthesis in toluenized Bacillus subtilis cells. Vigorous agitation of toluenized cells (localization test) demonstrated that the DNA replication is exclusively a cell-associated process. A DNA "repair" condition was also applied to toluenized cells and shown to be distinct from DNA replication in its DNA polymerase I dependency and its ability to synthesize DNA on template which is either cell associated or free, outside the cell. This repair condition was used in conjunction with the localization test to demonstrate the penetration of deoxyribonuclease I and possibly DNA polymerase I into toluenized cells. Therefore, we suggest that the localization test can be used to test the penetration of proteins into toluenized cells for both the DNA repair and replication processes.
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PMID:Tests for deoxyribonucleic acid synthesis in toluenized Bacillus subtilis cells. 420 14

2-(N-methylanilino)naphthalene-6-sulfonic acid (MANS) binds to G-actin at a single high affinity hydrophobic site (Kd = 41 microM). Salt-induced polymerization of MANS-G-actin results in a general enhancement of sample emission intensities at all wavelengths. At 430 nm, KCl-induced polymerization yields a 2,3-fold enhancement, while MgCl2-induced polymerization gives a 2.0-fold increase. Polymerization of MANS-G-actin in the absence of agitation produces MANS-F-actin samples that have fluorescence polarization values at 430 nm of 0.33. Subsequent mixing or sonication of such MANS-F-actin samples results in a dramatic drop in fluorescence polarization values to 0.14. After cessation of mixing, the polarization values do not recover to their initial levels. Circular polarization of luminescence studies on MANS-actin demonstrate that agitation of MANS-F-actin samples drastically alters emission anisotropy values. 9-Anthroyl choline (9AC) binds to G-actin at a single hydrophobic site (Kd = 68 microM). The fluorescence of 9AC-actin is sensitive to salt-induced polymerization and depends upon the identity of the salt employed. KCl causes a drop in the fluorescence intensity at 490 nm to 70% of the value for 9AC-G-actin, while MgCl2 produces a 30% increase in intensity. Polarization experiments with 9AC-actin produced qualitatively the same results as did those with MANS-actin. Differences in the behaviours of MANS-actin and 9AC-actin in response to polymerization by KCl and MgCl2 and in response to the binding of deoxyribonuclease I suggest that the binding sites on actin for MANS and 9AC do not overlap completely.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Fluorescence of actin-bound hydrophobic molecules. 662 8