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At least 307 records · Page 17Linked to original sources
PubMed1981

Antibody formation to dog pulp tissue altered by camphor paramonochlorophenol via the root canal.

Pulp tissue from three experimental dogs was tested for its antigenicity before and after incubation with CMCP. Reaction to Arthus skin tests showed an increased response to pulp that had been incubated in CMCP, washed, then injected, as compared with pulp or CMCP alone. Hemagglutinating antibody titers (1:360 to 1:450 dilutions) were obtained from pulp tissue altered by CMCP. Inhibition tests showed the specificity of the antibody to be at a dilution titer of 1:350. Therefore, CMCP altered dog pulp tissue and rendered it antigenically active, and a specific humoral response was produced.

Animals↗
PubMed2006

Asymmetric synthesis of alpha,alpha-disubstituted alpha-amino acids by diastereoselective alkylation of camphor-based tricyclic iminolactone.

A novel and convenient route for the preparation of chiral tricyclic iminolactones 9 and 10 from camphorquinone has been developed. Alkylation of iminolactones 9 and 10 provided iminolactones 16 and 17 in high yields which were, in turn, alkylated again to afford the alpha,alpha-disubstituted products in good yields (70-90%) and excellent diastereoselectivities (>98%). Hydrolysis of the alkylated iminolactones furnished the desired alpha,alpha-disubstituted alpha-amino acids in good yields and high enantiomeric excesses with good recovery yields of the chiral auxiliary 12 and 13. The extremely high endo-face selectivity for alkylation is discussed using semiempirical (MOPAC 93) calculations.

Alkylation↗
PubMed1997

Probing the interactions of putidaredoxin with redox partners in camphor P450 5-monooxygenase by mutagenesis of surface residues.

The role of surface amino acid residues in the interaction of putidaredoxin (Pdx) with its redox partners in the cytochrome P450cam (CYP101) system was investigated by site-directed mutagenesis. The mutated Pdx genes were expressed in Escherichia coli, and the proteins were purified and studied in vitro. Activity of the complete reconstituted P450cam system was measured, and kinetic parameters were determined. Partial assays were also conducted to determine the effect of the mutations on interactions with each redox partner. Some mutations altered interactions of Pdx with one redox partner but not the other. Other mutations affected interactions with both redox partners, suggesting some overlap in the binding sites on Pdx for putidaredoxin reductase and CYP101. Cysteine 73 of Pdx was identified as important in the interaction of Pdx with putidaredoxin reductase, whereas aspartate 38 serves a critical role in the subunit binding and electron transfer to CYP101.

Bacterial Proteins↗