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Biomedical subjects

D A Watts

Publications and source records attributed to D A Watts.

9 recordsLinked to original sources
PubMed2002

The genetic jigsaw of inflammatory bowel disease.

Following a prolonged period of relative inertia, real progress has been made in the past few years in understanding the pathogenesis of the chronic inflammatory bowel diseases, Crohn's disease and ulcerative colitis. Clinical experience, epidemiological studies, and molecular genetics have provided strong evidence that both genetic and environmental factors are important in disease pathogenesis, and gene-environmental interaction determines disease susceptibility and behaviour.

Antibodies, Monoclonal↗
PubMed1996

Reflux symptom relief with omeprazole in patients without unequivocal oesophagitis.

BACKGROUND: As many as 50% of patients with reflux symptoms have no endoscopic evidence of oesophagitis. This multicentre study was designed to assess symptom relief after omeprazole 20 mg once daily in patients with symptoms typical of gastro-oesophageal reflux disease but without endoscopic evidence of oesophagitis. METHODS: Patients (n = 209) were randomized in a double-blind study to receive either omeprazole 20 mg once daily (n = 98) or placebo (n = 111) for 4 weeks. Symptoms were assessed at clinic visits and using daily diary cards, with patient-completed questionnaires providing additional data on symptoms and on psychological disturbance. RESULTS: On completion, symptom relief favoured omeprazole: 57% of patients on omeprazole were free of heartburn (vs. 19% on placebo), 75% were free of regurgitation (47%) and 43% were completely asymptomatic (14%), each with P < 0.0001. Fewer patients in the omeprazole group required alginate/antacid relief medication (P < 0.05). Symptom relief (time to first heartburn-free day) was more rapid with omeprazole (2 vs. 5 days on placebo; P < 0.01). A greater reduction in anxiety occurred in the omeprazole group (P < 0.05). CONCLUSION: Omeprazole 20 mg once daily is effective in providing relief of the symptoms typical of gastro-oesophageal reflux disease in patients with essentially normal oesophageal mucosa.

Adult↗
PubMed1988

Split skin grafting using topical local anaesthesia (EMLA): a comparison with infiltrated anaesthesia.

The analgesic efficacy of EMLA cream was compared with that produced by infiltration of lignocaine solution when used to provide anaesthesia for cutting of skin grafts. The study was performed as an open parallel group comparison in 80 patients. Pain felt during administration of the anaesthetic and during cutting of the graft was assessed using visual analogue and verbal rating scales. During graft cutting, the anaesthesia produced by EMLA was at least as effective as infiltration. On administration, infiltration produced varying amounts of pain in all patients, but in contrast EMLA produced no discomfort. In view of this lack of discomfort and the consequent greater freedom afforded regarding the area of donor site anaesthetised, EMLA can be considered the treatment of choice when skin grafts are harvested under local anaesthetic.

Administration, Cutaneous↗
PubMed1986

Myoglobin interspecies structural differences: effects on autoxidation and oxygenation.

Thermodynamic and kinetic parameters of the oxygenation and autoxidation reactions were determined for yellowfin tuna (Thunnus albacares), Pacific green sea turtle (Chelonia mydas caranigra), and sperm whale myoglobin. These proteins have quite similar heme contact residues, but vary in residues which are involved in globin stabilization and in postulated ligand paths to the heme iron. Oxygen equilibria measurements from 10 to 40 degrees C reveal that green sea turtle myoglobin has a lower oxygen affinity and lower enthalpy and entropy for oxygen-binding than the other proteins. Yellowfin tuna myoglobin has the most rapid oxygen dissociation rate and the highest susceptibility to autoxidation under all conditions studied. However, the dependence of the autoxidation rate on ionic strength is the same for the three proteins, despite substantial differences in their dynamic stabilities. These results suggest that the autoxidation reaction is more dependent on ligand accessibility than on the dynamic stability of the myoglobin.

Animals↗
PubMed1983

The primary structure of myoglobin from pacific green sea turtle (Chelonia mydas caranigra).

The amino acid sequence of the main component myoglobin from skeletal muscle of Pacific green sea turtle (Chelonia mydas caranigra) has been determined. The globin is 153 residues in length and has a free amino-terminus. The heme-binding and internal residues are as found in mammalian myoglobins. Ten substitutions are observed between this myoglobin and that from map turtle. About 38, 52, 47 and 86 substitutions are noted in comparison with the myoglobins of other reptiles, mammals, birds and fish, respectively. The inferred pattern of structural stabilization and conservation of two loci are typical of tetrapod myoglobin.

Alligators and Crocodiles↗
PubMed1980

The primary structure of myoglobin from yellowfin tuna (Thunnus albacares).

The amino acid sequence of myoglobin from yellowfin tuna (Thunnus albacares) has been determined. The globin is an aminoacetylated chain containing 146 residues and having deletions, with respect to mammalian and avian myoglobins, at the NH2 terminus and two internal locations. From 79 to 85 amino acid substitutions are observed between this myoglobin and those of mammals, birds, and shark. Two external regions containing 6 and 7 residues, which are highly conserved in mammalian and avian myoglobins, are greatly or totally altered in the tuna sequence. Significant differences are apparent in the extent of electrostatic bonding in the myoglobins of fish and in those of mammals or birds.

Amino Acid Sequence↗
PubMed1979

Sequences of the soluble tryptic peptides from myoglobin of yellowfin tuna (Thunnus albacares).

1. Amino acid sequences of the soluble tryptic peptides of yellowfin tuna myoglobin, comprising 60% of the total residues, are presented. 2. The amino terminus is acetylated as shown by Fourier transform nuclear magnetic resonance spectroscopy of an N-terminal dipeptide. 3. Comparison of peptide sequences from yellowfin tuna myoglobin with corresponding regions of mammalian myoglobins shows obvious homology around the heme-attachment site and the carboxyl terminus, but marked dissimilarity is evident at other locations, such as the amino terminal region.

Acetylation↗