salicylates and 2-4-di-tert-butylphenol

salicylates has been researched along with 2-4-di-tert-butylphenol* in 2 studies

Other Studies

2 other study(ies) available for salicylates and 2-4-di-tert-butylphenol

Article	Year
Function and immunocytochemical localization of two novel odorant-binding proteins in olfactory sensilla of the scarab beetle Holotrichia oblita Faldermann (Coleoptera: Scarabaeidae). Chemical senses, 2012, Volume: 37, Issue:2 Odorant-binding proteins (OBPs) are found in both insects and vertebrates, and it is believed that they are involved in chemical communication. In this study, we identify and express 2 OBPs from the scarab beetle, Holotrichia oblita Faldermann (Coleoptera: Scarabaeidae). HoblOBP1 shows more similarities with other scarab beetle OBPs, whereas HoblOBP2 is more diverse. N-phenyl-1-naphthylamine (1-NPN) is used as a fluorescent probe in ligand-binding experiment, and results indicate that both HoblOBPs prefer plant volatiles to putative H. oblita sex pheromones. HoblOBP1 shows binding affinity to a wider range of test compounds, but HoblOBP2 displays more specific binding affinity. Cinnamaldehyde and 2,4-di-tert-butylphenol bind to HoblOBP1 can elicit strong electrophysiological responses of the antennae from female H. oblita adults, respectively. Methyl salicylate also shows good affinity to HoblOBP2 and it can elicit moderate electrophysiological responses. Although, β-ionone is one of the ligands of the strongest binding, it elicits a weak electrophysiological response. In the immunocytochemical analysis, we observe that HoblOBP1 and HoblOBP2 are coexpressed in sensilla basiconica and placodea in both sexes. Topics: 1-Naphthylamine; Acrolein; Amino Acid Sequence; Animals; Arthropod Antennae; Coleoptera; Female; Insect Proteins; Male; Molecular Sequence Data; Norisoprenoids; Phenols; Phylogeny; Protein Binding; Protein Isoforms; Receptors, Odorant; Recombinant Proteins; Salicylates; Sensilla; Sex Attractants; Smell; Substrate Specificity	2012
On the Kolbe-Schmitt synthesis of pharmacologically useful salicylates: carboxylation of 2,4-di-t-butylphenol and identification and reduction of the formation of 2,2'-dihydroxy-3,3',5,5'-tetra-t-butylbiphenyl in the synthesis of 3,5-di-t-butylsalicylic a Journal of pharmaceutical sciences, 1991, Volume: 80, Issue:8 The initial yield of 3,5-di-t-butylsalicylic acid obtained via Kolbe-Schmitt carboxylation of the potassium salt of 2,4-di-t-butylphenol was less than 1% and was accompanied by a 65% yield of 2,2'-dihydroxy-3,3',5,5'- tetra-t-butylbiphenyl, a dimer of the 2,4-di-t-butylphenol formed by ortho coupling of phenoxide radicals. Formation of this dimer was decreased to 8%, and the yield of 3,5-di-t-butylsalicylic acid was increased to 68% by optimizing reaction time and temperature and decreasing the amount of oxygen present during carboxylation. This modification of the Kolbe-Schmitt reaction conditions may be generally helpful in the synthesis of all pharmacologically useful salicylates. Topics: Biphenyl Compounds; Oxidation-Reduction; Phenols; Salicylates; Temperature	1991

Article

Year

Function and immunocytochemical localization of two novel odorant-binding proteins in olfactory sensilla of the scarab beetle Holotrichia oblita Faldermann (Coleoptera: Scarabaeidae).

Chemical senses, 2012, Volume: 37, Issue:2

Odorant-binding proteins (OBPs) are found in both insects and vertebrates, and it is believed that they are involved in chemical communication. In this study, we identify and express 2 OBPs from the scarab beetle, Holotrichia oblita Faldermann (Coleoptera: Scarabaeidae). HoblOBP1 shows more similarities with other scarab beetle OBPs, whereas HoblOBP2 is more diverse. N-phenyl-1-naphthylamine (1-NPN) is used as a fluorescent probe in ligand-binding experiment, and results indicate that both HoblOBPs prefer plant volatiles to putative H. oblita sex pheromones. HoblOBP1 shows binding affinity to a wider range of test compounds, but HoblOBP2 displays more specific binding affinity. Cinnamaldehyde and 2,4-di-tert-butylphenol bind to HoblOBP1 can elicit strong electrophysiological responses of the antennae from female H. oblita adults, respectively. Methyl salicylate also shows good affinity to HoblOBP2 and it can elicit moderate electrophysiological responses. Although, β-ionone is one of the ligands of the strongest binding, it elicits a weak electrophysiological response. In the immunocytochemical analysis, we observe that HoblOBP1 and HoblOBP2 are coexpressed in sensilla basiconica and placodea in both sexes.

Topics: 1-Naphthylamine; Acrolein; Amino Acid Sequence; Animals; Arthropod Antennae; Coleoptera; Female; Insect Proteins; Male; Molecular Sequence Data; Norisoprenoids; Phenols; Phylogeny; Protein Binding; Protein Isoforms; Receptors, Odorant; Recombinant Proteins; Salicylates; Sensilla; Sex Attractants; Smell; Substrate Specificity

2012

On the Kolbe-Schmitt synthesis of pharmacologically useful salicylates: carboxylation of 2,4-di-t-butylphenol and identification and reduction of the formation of 2,2'-dihydroxy-3,3',5,5'-tetra-t-butylbiphenyl in the synthesis of 3,5-di-t-butylsalicylic a

Journal of pharmaceutical sciences, 1991, Volume: 80, Issue:8

The initial yield of 3,5-di-t-butylsalicylic acid obtained via Kolbe-Schmitt carboxylation of the potassium salt of 2,4-di-t-butylphenol was less than 1% and was accompanied by a 65% yield of 2,2'-dihydroxy-3,3',5,5'- tetra-t-butylbiphenyl, a dimer of the 2,4-di-t-butylphenol formed by ortho coupling of phenoxide radicals. Formation of this dimer was decreased to 8%, and the yield of 3,5-di-t-butylsalicylic acid was increased to 68% by optimizing reaction time and temperature and decreasing the amount of oxygen present during carboxylation. This modification of the Kolbe-Schmitt reaction conditions may be generally helpful in the synthesis of all pharmacologically useful salicylates.

Topics: Biphenyl Compounds; Oxidation-Reduction; Phenols; Salicylates; Temperature

1991