Melting point standard 182-184 °C, p-anisic acid is useful for the regular assessment of identity or purity of a substance. Its value is determined as an average of 6 to 12 measurements with a Büchi B-545 instrument that is calibrated against primary standards.
Application
This product is an analytical standard used as a melting point calibration standard.
Features and Benefits
Traceable to primary standards from LGC, London
Grade: Analytical Standard
Melting point standardized in the thermodynamic mode of analysis
Standard deviation up to ± 0.3 °C
Documented with certificates of analysis and safety data sheet
Dalton transactions (Cambridge, England : 2003), 41(28), 8703-8714 (2012-06-15)
The crystal structures of the 4-methoxybenzoate bound forms of cytochrome P450 enzymes CYP199A2 and CYP199A4 from the Rhodopseudomonas palustris strains CGA009 and HaA2 have been solved. The structures of these two enzymes, which share 86% sequence identity, are very similar
Journal of natural products, 64(12), 1556-1558 (2002-01-05)
From the hydrophilic extract of the ascidian Polycarpa aurata three new compounds, N-(4-methoxybenzoyl)-N'-methylguanidine (1), butyl 2-(4-methoxyphenyl)-2-oxoacetate (2), and 2-(4-methoxyphenyl)-N-methyl-2-oxoacetamide (3), together with the known compounds methyl 2-(4-methoxyphenyl)-2-oxoacetate (4) and 4-methoxybenzoic acid were isolated. The structures of all isolates were determined
Applied microbiology and biotechnology, 52(6), 834-838 (2000-01-05)
Ligninolytic basidiomycetes were screened for their ability to reduce aryl acids to the corresponding aldehydes and alcohols. Seven fungal strains converted p-anisic acid in high molar yields to the reduced products. The white-rot fungus Bjerkandera sp. strain BOS55 was one
Journal of bacteriology, 175(5), 1467-1474 (1993-03-01)
A red-pigmented coryneform bacterium, identified as Rhodococcus rhodochrous strain 116, that grew on 2-ethoxyphenol and 4-methoxybenzoate as sole carbon and energy sources was isolated. Phylogenetic analysis based on the 16S rDNA sequences indicates that the strain clusters more closely to
The Journal of biological chemistry, 284(37), 24840-24847 (2009-07-04)
Aryl-alcohol oxidase (AAO) is a FAD-containing enzyme in the GMC (glucose-methanol-choline oxidase) family of oxidoreductases. AAO participates in fungal degradation of lignin, a process of high ecological and biotechnological relevance, by providing the hydrogen peroxide required by ligninolytic peroxidases. In
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