Co-purification of gastric mucoproteins with DNA: an explanation for the reported 'interaction' of omeprazole with DNA in rat tissues. Longitudinal oesophageal muscle and pharyngo-oesophageal dysphagia--a deductive study. Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport. Rx drugs

Drugs online research references

Mutat Res. 1994 Oct;322(4):307-20.
Co-purification of gastric mucoproteins with DNA: an explanation for the reported 'interaction' of omeprazole with DNA in rat tissues.

Adams SP, Laws GM, Storer RD, Kraynak AR, DeLuca JG, Nichols WW.

Merck Research Laboratories, West Point, PA 19486.

Recently, Phillips et al. reported that small amounts of radioactivity derived from [14C]omeprazole were 'associated' with DNA purified from gastrointestinal tissues of treated rats (Mutagenesis 7, 277-283, 1992). We hypothesized that this radioactivity arose from omeprazole bound to contaminating protein in the DNA fraction (Mutagenesis 7, 395-396, 1992). Using rats injected with 35S-labeled amino acids, we found significant protein contamination (0.06 microgram of protein per microgram of DNA) in DNA purified from gastrointestinal tissues. Gastric mucous proteins represent likely candidates for binding of omeprazole in the rat model used by Phillips et al. To investigate this, we partially purified proteins from gastric mucus, incubated them with [14C]omeprazole, and then added these radiolabeled mucoproteins to homogenates of rat colon and duodenum before starting the DNA purification. Detectable amounts of the added mucoproteins remained in the DNA fraction, but none of the control protein, bovine serum albumin, remained with the DNA. Further characterization of the mucoproteins by hydroxyapatite chromatography indicated that a certain population of these proteins survived the DNA purification procedures. These data indicate that the association of omeprazole with DNA reported by Phillips et al. most probably is explained by binding of omeprazole to mucous glycoproteins (or other proteins present in the GI tract) that selectively survive DNA purification protocols.

online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7523925&dopt=Abstract

note: kwd match prilosec online literature

Acta Otolaryngol Suppl. 2000;543:239-40.
Longitudinal oesophageal muscle and pharyngo-oesophageal dysphagia--a deductive study.

Grahn LT.

Department of Neuroscience and Locomotion, University Hospital, Linkoping, Sweden.

The hypothesis has been raised that a dysfunction of the longitudinal oesophageal muscle is the common denominator for pharyngeal and oesophageal dysphagia in patients with hiatal hernia, and that contraction of the longitudinal muscle is a contributing factor for the opening of the upper oesophageal sphincter and for the stiffening of the oesophageal wall when swallowing. Different studies were used to test the implications of this hypothesis. It was concluded that dysfunction of the longitudinal oesophageal muscle, caused by slipping of the distal end through the hiatal canal, can explain oesophageal dysphagia and inadequate opening of the upper oesophageal sphincter.

online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10909030&dopt=Abstract

note: kwd match prilosec online literature

Mol Microbiol. 1995 Jan;15(1):97-106.
Nucleotide sequence and mutational analysis indicate that two Helicobacter pylori genes encode a P-type ATPase and a cation-binding protein associated with copper transport.

Ge Z, Hiratsuka K, Taylor DE.

Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton, Canada.

A 2.7 kb fragment of Helicobacter pylori UA802 chromosomal DNA was cloned and sequenced. Three open reading frames (designated ORF1, ORF2 and ORF3, respectively) were predicted from the DNA sequence, of which ORF1 and ORF2 appeared to be located within the same operon. The deduced 611-amino-acid sequence of ORF1, a P-type ATPase (designated hpCopA), had striking homology (29-38%) with several bacterial P-type ATPase and contained the potential functional domains conserved in P-type ATPases from various sources ranging from bacterial to human. A protein of 66 amino acids (designated hpCopP) encoded by ORF2 shared extensive sequence similarity with MerP, a periplasmic mercuric ion-transporting protein, and contains the heavy metal-binding motif. Disruption of ORF1 with a chloramphenicol-resistance cassette (CAT) rendered the H. pylori mutants more susceptible to cupric ion than their parental strains, whereas there is no significant alteration of susceptibility to Ni2+, Cd2d+ and Hg2+ between the mutants and the parental strains. The results obtained indicate that ORF1 and ORF2 comprise a cation-transporting system which is associated with copper export out of the H. pylori cells.

online pharmacy ref source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7752900&dopt=Abstract

note: kwd match prilosec online literature

Herbs and Pharmaceuticals Online || Hair Million herbal formula for hair loss and hair growth || Antibiotics and prescription medications online literature ||