Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Hydroxybenzoates”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 469 records · Page 26Linked to original sources
PubMed1982

[Synthesis of phenol-antigen conjugates by reacting N-hydroxysuccinimidic esters of hydroxybenzoic acids with human serum albumin and bovine gamma globulin].

Salicylic acid, beta-resorcylic acid and gentisic acid were acetylated and then reacted with N-hydroxysuccinimide according to the DDC procedure to give the corresponding activated esters. The reaction of these N-hydroxysuccinimidic esters with human serum albumin and bovine gamma globulin yielded modified proteins containing hydroxybenzoyl residues linked to amino groups, the mode of linkage being of the acid amide type.

Acetylation↗
PubMed1995

Plasmid mutagenesis by PCR for high-level expression of para-hydroxybenzoate hydroxylase.

We report a PCR deletion mutagenesis method for the exact positioning of a foreign gene (pobA) in the lac operon of an expression plasmid in place of the lacZ protein code. This method requires the synthesis of four oligonucleotides and three PCR reactions to delete unwanted bases and retain the nucleotide sequence naturally found between the lac promoter and the protein code. The engineered plasmid results in the production of at least 40% of the cellular protein as the foreign polypeptide. In the example presented the expression of the protein is high even with a substantial difference in codon usage between the host (Escherichia coli) and a foreign gene from Pseudomonas aeruginosa. Some of the polypeptide produced has the ame properties as native protein and is easily purified. The remainder is present as insoluble inclusion bodies. This method of plasmid refinement may be applicable to the expression of many proteins.

4-Hydroxybenzoate-3-Monooxygenase↗