Soluble in Chloroform,Dichloromethane,Ethyl Acetate,DMSO,Acetone,etc.
544.3±50.0 °C at 760 mmHg
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provides coniferyl ferulate(CAS#:2643-85-8) MSDS, density, melting point, boiling point, structure, formula, molecular weight etc. Articles of coniferyl ferulate are included as well.>> amp version: coniferyl ferulate
Affinity purified, polyclonal antibodies were prepared against three tektins (tektins A, B, and C) isolated from sea urchin sperm axonemal microtubules. These antibodies (anti-tektins) were used to localize tektins in axonemes, basal bodies, and centrioles. By immunofluorescence microscopy it could be demonstrated that in sperm tails from Lytechinus pictus all three anti-tektins stain all nine axonemal doublet microtubules and A-tubule extensions along their entire length. In addition to staining doublet microtubules, anti-tektin C weakly labeled the central-pair microtubules in sperm tails from Patiria miniata. The anti-tektin staining revealed also a clear cross-reaction with basal bodies of sea urchin sperm and with centrioles of cells from hamsters, humans, and pigs. These data provide evidence of tektin or tektin-like proteins in basal bodies and centrioles and suggest that centriole microtubules are constructed according to the same principles as flagellar microtubules.
Evidence for tektins in centrioles and axonemal microtubules.
W Steffen and R W Linck
The unr gene was identified as a transcription unit located immediately upstream of N-ras in the genome of several mammalian species. While this genetic organization could be important for the transcriptional regulation of unr and N-ras, the function of the protein product of unr is unknown. unr is ubiquitously expressed and codes for an 85 kDa protein which is not closely related to previously characterized proteins. Nevertheless, a search for protein motifs has indicated the presence of five ‘cold shock domains’ within unr, a motif present in procaryotic cold shock proteins and in the vertebrate Y box factors. As these proteins have been reported to interact with nucleic acids, we investigated whether unr could bind to some classes of nucleic acids. We report here that unr has a high affinity for single-stranded DNA or RNA and a low affinity for double-stranded nucleic acids. Its low affinity for double-stranded DNA clearly distinguishes unr from the Y box factors. The binding of unr to RNA does not appear to depend upon extended sequence motifs but requires some level of sequence complexity as unr has only a low affinity for most simple polymers including polyA stretches. unr is also characterized by its low affinity for double-stranded and structured RNAs. We further determined that unr is mostly localized in the cytoplasm, and is in part associated with the endoplasmic reticulum. These studies indicate that unr is a novel single-stranded nucleic acid binding protein which is likely to be associated with cytoplasmic mRNA in vivo.
Nucleic acid binding and intracellular localization of unr, a protein with five cold shock domains.
H Jacquemin-Sablon, G Triqueneaux, S Deschamps, M le Maire, J Doniger, and F Dautry
1994 Jul 11;
Pseudomonas putida F1 and Pseudomonas sp. strain JS150 initiate toluene degradation by incorporating molecular oxygen into the aromatic nucleus to form cis-1,2-dihydroxy-3-methylcyclohexa-3,5-diene. When toluene-grown cells were incubated with 2- and 3-nitrotoluene, the major products identified were 2- and 3-nitrobenzyl alcohol, respectively. The same cells oxidized 4-nitrotoluene to 2-methyl-5-nitrophenol and 3-methyl-6-nitrocatechol. Escherichia coli JM109(pDTG601), which contains the toluene dioxygenase genes from P. putida F1 under the control of the tac promoter, oxidized the isomeric nitrotoluenes to the same metabolites as those formed by P. putida F1 and Pseudomonas sp. strain JS150. These results extend the range of substrates known to be oxidized by this versatile enzyme and demonstrate for the first time that toluene dioxygenase can oxidize an aromatic methyl substituent.
Oxidation of nitrotoluenes by toluene dioxygenase: evidence for a monooxygenase reaction.
J B Robertson, J C Spain, J D Haddock, and D T Gibson