BackgroundAs health care has increased in complexity and health care teams have been offered as a solution, so too is there an increased need for stronger interprofessional collaboration. However the intraprofessional factions that exist within every profession challenge interprofessional communication through contrary paradigms. As a contender in the conservative spinal health care market, factions within chiropractic that result in unorthodox practice behaviours may compromise interprofessional relations and that profession’s progress toward institutionalization. The purpose of this investigation was to quantify the professional stratification among Canadian chiropractic practitioners and evaluate the practice perceptions of those factions.MethodsA stratified random sample of 740 Canadian chiropractors was surveyed to determine faction membership and how professional stratification could be related to views that could be considered unorthodox to current evidence-based care and guidelines. Stratification in practice behaviours is a stated concern of mainstream medicine when considering interprofessional referrals.ResultsOf 740 deliverable questionnaires, 503 were returned for a response rate of 68%. Less than 20% of chiropractors (18.8%) were aligned with a predefined unorthodox perspective of the conditions they treat. Prediction models suggest that unorthodox perceptions of health practice related to treatment choices, x-ray use and vaccinations were strongly associated with unorthodox group membership (X2 =13.4, p = 0.0002).ConclusionChiropractors holding unorthodox views may be identified based on response to specific beliefs that appear to align with unorthodox health practices. Despite continued concerns by mainstream medicine, only a minority of the profession has retained a perspective in contrast to current scientific paradigms. Understanding the profession’s factions is important to the anticipation of care delivery when considering interprofessional referral.

PhyA from Selenomonas ruminantium (PhyAsr), is a bacterial protein tyrosine phosphatase (PTP)-like inositol polyphosphate phosphatase (IPPase) that is distantly related to known PTPs. PhyAsr has a second substrate binding site referred to as a standby site and the P-loop (HCX 5 R) has been observed in both open (inactive) and closed (active) conformations. Site-directed mutagenesis and kinetic and structural studies indicate PhyAsr follows a classical PTP mechanism of hydrolysis and has a broad specificity toward polyphosphorylated myo-inositol substrates, including phosphoinositides. Kinetic and molecular docking experiments demonstrate PhyAsr preferentially cleaves the 3-phosphate position of Ins P 6 and will produce Ins(2)P via a highly ordered series of sequential dephosphorylations: D-Ins(1,2,4,5,6)P 5 , Ins(2,4,5,6)P 4 , D-Ins(2,4,5)P 3 , and D-Ins(2,4)P 2 . The data support a distributive enzyme mechanism and suggest the PhyAsr standby site is involved in the recruitment of substrate. Structural studies at physiological pH and high salt concentrations demonstrate the ''closed'' or active P-loop conformation can be induced in the absence of substrate. These results suggest PhyAsr should be reclassified as a D-3 myo-inositol hexakisphosphate phosphohydrolase and suggest the PhyAsr reaction mechanism is more similar to that of PTPs than previously suspected.Keywords: inositol polyphosphate phosphatase; protein tyrosine phosphatase; phosphoinositide phosphatase; phytase; myo-inositol; P-loop; hydrolysis pathway Supplemental material: see www.proteinscience.org Protein tyrosine phosphatase (PTP) superfamily enzymes have been discovered in a range of prokaryotes, and most appear to serve roles that mimic their better-known eukaryotic counterparts as regulators of cellular function (Shi et al. 1998;Kennelly and Potts 1999). Some bacteria have adapted PTPs as ''molecular missiles,'' secreted into the infected host where they assist in the progression of infection (Bliska et al. 1991;Fu and Galan 1998;Bretz et al. 2003). The recently described PTP-like inositol polyphosphate phosphatase (IPPase) from Selenomonas ruminantium, PhyAsr, contains a PTP-like active site signature sequence (HCEAGVGR) but lacks significant primary sequence identity with known IPPases and PTPs (<20%). While its biological function is unclear, it is the first example of a PTP-like enzyme with activity toward myo-inositol hexakisphosphate (Ins P 6 , Fig. 1), one of the most abundant inositol polyphosphates (IPPs) in a majority of prokaryotic and eukaryotic cells (Sasakawa et al. 1995).The X-ray crystallographic structure of PhyAsr (Chu et al. 2004) reveals a PTP-like fold and several novel 4 These authors contributed equally to this work. Reprint requests to: Steven C. Mosimann, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta T1K 3M4, Canada; e-mail: steven.mosimann@uleth.ca; fax: (403) 329-2057.Article published online ahead of print. Article and publication date are at http://www.proteinscien...

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