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At least 1,783 records · Page 99Linked to original sources
PubMed2000

Emergency medicine and "acute" general practice: comparing apples with oranges.

Emergency Departments (EDs) operate at the interface between the inpatient and ambulatory sectors of health care. Because of shared funding between the Commonwealth and States for ambulatory care, there has been intense focus on the ED patient population, and the potential to shift the locus of care for non-inpatients. One of the frequently cited models for the provision of after-hours GP services is the Balmain General Practice Casualty (GPC). This paper analyses the GPC model, looking in detail at casemix, clinical quality, waiting times and cost-effectiveness. It is argued that the services provided and the casemix of the patient population of GPC and EDs are distinctly different. Cost-effectiveness for GPC has not been objectively established. Health service planning should recognise the distinct but complementary roles of general practice and emergency medicine. Evaluation of alternative models of service provision should critically examine the available evidence, and comparisons should be based on a precise analysis of equivalent services.

Cost-Benefit Analysis↗
PubMed1996

A binding site for thrombin in the apple 1 domain of factor XI.

Previously we defined a binding site for high molecular weight kininogen (HK) in the A1 domain of factor XI (FXI). Since thrombin can activate FXI and HK inhibits the activation of FXI by thrombin, we have identified a thrombin binding site in FXI. Both the recombinant A1 domain (Glu1-Ser90) and a synthetic peptide (Phe56-Ser86) containing the HK binding site inhibited FXI activation by thrombin. Both a monoclonal antibody, 5F7, recognizing the A1 domain, and the rA1 domain were shown to be competitive inhibitors of thrombin-catalyzed FXI activation. The peptides Ala45-Arg54 and Val59-Arg70 acted synergistically to inhibit FXI activation by thrombin. Mutant rA1 domain constructs (Val64 --> Ala and Ile77 --> Ala), which do not inhibit FXI binding to HK, retain full capacity to inhibit FXI activation by thrombin. The peptide Ala45-Arg54 inhibited thrombin-catalyzed FXI activation, whereas it had no effect on FXI binding to HK. In contrast, the peptide Asn72-Leu83 (which inhibited FXI binding to HK) did not inhibit FXI activation by thrombin. Thus, a thrombin binding site exists in the A1 domain of FXI spanning residues Ala45-Arg70 that is contiguous with but separate and distinct from the HK binding site. These sites may regulate which ligand is bound to FXI and through which pathway FXI is activated.

Amino Acid Sequence↗
PubMed1999

Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX.

Activated coagulation factor XI (factor XIa) proteolytically cleaves its substrate, factor IX, in an interaction requiring the factor XI A3 domain (Sun, Y., and Gailani, D. (1996) J. Biol. Chem. 271, 29023-29028). To identify key amino acids involved in factor IX activation, recombinant factor XIa proteins containing alanine substitutions for wild-type sequence were expressed in 293 fibroblasts and tested in a plasma clotting assay. Substitutions for Ile(183)-Val(191) and Ser(195)-Ile(197) at the N terminus and for Ser(258)-Ser(264) at the C terminus of the A3 domain markedly decreased factor XI coagulant activity. The plasma protease prekallikrein is structurally homologous to factor XI, but activated factor IX poorly. A chimeric factor XIa molecule with the A3 domain replaced with A3 from prekallikrein (FXI/PKA3) activated factor IX with a K(m) 35-fold greater than that of wild-type factor XI. FXI/PKA3 was used as a template for a series of proteins in which prekallikrein A3 sequence was replaced with factor XI sequence to restore factor IX activation. Clotting and kinetics studies using these chimeras confirmed the results obtained with alanine mutants. Amino acids between Ile(183) and Val(191) are necessary for proper factor IX activation, but additional sequence between Ser(195) and Ile(197) or between Phe(260) and Ser(265) is required for complete restoration of activation.

Amino Acid Sequence↗
PubMed2004

The influence of 5% and 10% dietary apple pectin on parameters of fermentation in faeces and caecal digesta of weaning pigs.

In order to determine the effect of pectin on fermentation parameters in the faeces and caecal digesta of weaned pigs 18 castrated male crossbred pigs with an average body weight of 8 kg were fitted with T-cannulas at the caecum. The animals were randomly distributed into three groups and fed with diets supplemented with 0, 5 and 10% pectin. Faeces were collected over a period of 3 days. Thereafter the diets were withdrawn for 24 h followed by ad libitum feeding to enhance the feed intake. Caecal chyme was collected 0, 8 and 24 h postprandial. In the faeces the addition of 5% pectin to the diet lowered the content of dry matter and lactic acid. The pH and the digestibility of pectins, the concentration of total SCFA, acetate, propionate, butyrate, bicarbonate and chloride increased. Dietary pectin of 10% increased the content of total SCFA and acetate further. When the diets were withdrawn and fed ad libitum 24 h later, a decline of the pH and an increased concentration of lactate in the caecal chyme could be observed in all groups up to 8 h after feeding. With an interval of 8 to 24 h after feeding, a further decline in pH and a rise of lactate only occurred when the diet was not supplemented with pectin. It was concluded that pectin might be beneficial for the development of fermentative processes in the large intestine.

Animals↗
PubMed2001

From aardvarks to apples and orchids to ostriches: the simple evolutionary roots of a world of biological complexity and biodiversity.

Most genes arise by gene duplication, a process that has allowed the evolutionary development of new proteins and peptides with diverse functions, based on modifications of pre-existing sequences. Gene duplication creates both new DNA substrate for the encoding of information, and an information substrate for further modification of already evolved information. Because DNA "wants" to copy itself, both vertically from generation to generation and horizontally due to gene duplication, it creates a great deal of nonsense within the genome called "junk" or "selfish" DNA, which has no present function. However, it acts as an inadvertent evolutionary library and as an autocatalytic substrate for the creation of more DNA containing already-preselected sequences. The process, over evolutionary time, has created large families of related hormones, regulatory peptides, and their receptor and signaling systems, for many of which the functions have yet to be described.

Animals↗