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  • 1995-1999  (3)
  • mass spectrometry  (2)
  • Crohn's disease  (1)
  • [abr] PFC; plaque-forming cell
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Diseases of the colon & rectum 41 (1998), S. 1293-1296 
    ISSN: 1530-0358
    Keywords: Crohn's disease ; Recurrence ; Stapled anastomosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract PURPOSE: Perianastomotic recurrence after resection in Crohn's disease may be related to ischemia and subacute obstruction at the anastomosis. A technique designed to minimize these factors currently is being evaluated. METHODS: From 1984 to 1997 69 patients underwent resection and primary anastomosis for symptomatic Crohn's disease (17 jejunal or ileal, 72 ileocolic, and 7 colocolic resections). Of these, 42 patients underwent functional end-to-end anastomoses with the use of linear cutting staplers (ProximateTM 75 mm or GIA 228 80 mm) and 27 patients underwent end-to-end sutured anastomoses. RESULTS: In the stapled anastomosis group one (2 percent) patient required reoperation for recurrent symptoms at 46 months. Complications occurred in four (8 percent) patients (one enterocutaneous fistula, one wound infection, one abscess, and one ileus). There were no anastomotic leaks. The median postoperative stay was seven (range, 5–26) days. In the sutured anastomosis group 14 (43 percent) patients required 15 further resections for symptomatic recurrence at a median of 46 (range, 4–91) months. Complications occurred in six (17 percent) patients (two anastomotic leaks, two fistulas, one stricture, and one pulmonary embolus). The median postoperative stay was 10 (range, 6–28) days. CONCLUSIONS: Functional end-to-end stapled anastomoses after resection for Crohn's disease may be associated with fewer complications than sutured anastomoses and may delay reoperation for symptomatic recurrence. Further evaluation of the technique is indicated.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0887-3585
    Keywords: mass spectrometry ; time-of-flight ; nanoflow electrospray ; transthyretin ; retinol binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Complexes formed between transthyretin and retinol-binding protein prevent loss of retinol from the body through glomerular filtration. The interactions between these proteins have been examined by electrospray ionization combined with time-of-flight mass analysis. Conditions were found whereby complexes of these proteins, containing from four to six protein molecules with up to two ligands, are preserved in the gas phase. Analysis of the mass spectra of these multimeric species gives the overall stoichiometry of the protein subunits and provides estimates for solution dissociation constants of 1.9 ± 1.0 × 10-7 M for the first and 3.5 ± 1.0 × 10-5 M for the second retinol-binding protein molecule bound to a transthyretin tetramer. Dissociation of these protein assemblies within the gas phase of the mass spectrometer shows that each retinol-binding protein molecule interacts with three transthyretin molecules. Mass spectral analysis illustrates not only a correlation with solution behavior and crystallographic data of a closely related protein complex but also exemplifies a general method for analysis of multi-protein assemblies. Proteins Suppl. 2:3-11, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 3
    ISSN: 0887-3585
    Keywords: mass spectrometry ; time-of-flight ; nanoflow electrospray ; transthyretin ; retinol binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Complexes formed between transthyretin and retinol-binding protein prevent loss of retinol from the body through glomerular filtration. The interactions between these proteins have been examined by electrospray ionization combined with time-of-flight mass analysis. Conditions were found whereby complexes of these proteins, containing from four to six protein molecules with up to two ligands, are preserved in the gas phase. Analysis of the mass spectra of these multimeric species gives the overall stoichiometry of the protein subunits and provides estimates for solution dissociation constants of 1.9 ± 1.0 × 10-7 M for the first and 3.5 ± 1.0 × 10-5 M for the second retinol-binding protein molecule bound to a transthyretin tetramer. Dissociation of these protein assemblies within the gas phase of the mass spectrometer shows that each retinol-binding protein molecule interacts with three transthyretin molecules. Mass spectral analysis illustrates not only a correlation with solution behavior and crystallographic data of a closely related protein complex but also exemplifies a general method for analysis of multi-protein assemblies. Proteins Suppl. 2:3-11, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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