Journal: Journal of Minimal Access Surgery

Article Title: Breakage of fascial closure device during laparoscopic surgery

doi: 10.4103/0972-9941.16533

Figure Lengend Snippet: (A) Lower jaw of the Berci fascial closure device is continuous with the shaft (arrow in inset). (B) Broken tip (arrow) comprising upper and lower jaws soldered on to the body of the indigenous fascial closure device

Article Snippet: After the adverse incident reported above, we carefully inspected the tips of the Berci FCD (Karl Storz, Tuttlingen, Germany) ( ) and also of the indigenous device manufactured locally that was used in our patient ( ).

Techniques:

Journal:

Article Title: Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms

doi: 10.1016/j.bone.2009.07.009

Figure Lengend Snippet: Kcat/KM for the four BALP isoforms using the synthetic substrate pNPP at pH 9.8 and at 7.4. The BALP B2 isoform had 35-fold higher activity than the B1 isoform for pNPP at pH 9.8. The same trend was observed with pNPP at pH 7.4. The catalytic activities were higher at pH 9.8, but lower at pH 7.4, when the BALP isoforms were treated with neuraminidase. ■ = BALP isoforms treated with neuraminidase.

Article Snippet: We thank Philippe Crine at Enobia Pharma for the generous contribution of the recombinant BALP isoform sALP-FcD 10 .

Techniques: Activity Assay

Journal:

Article Title: Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms

doi: 10.1016/j.bone.2009.07.009

Figure Lengend Snippet: Catalytic activity for the BALP isoforms using different substrates

Article Snippet: We thank Philippe Crine at Enobia Pharma for the generous contribution of the recombinant BALP isoform sALP-FcD 10 .

Techniques: Activity Assay

Journal:

Article Title: Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms

doi: 10.1016/j.bone.2009.07.009

Figure Lengend Snippet: Kcat/KM for the four BALP isoforms using the three suggested endogenous substrates: inorganic pyrophosphate (PPi), pyridoxal 5′-phosphate (PLP) and phosphoethanolamine (PEA) at pH 7.4. B2 had the highest activity for all the natural substrates. The catalytic activity for PEA was barely detectable for all four BALP isoforms. ■ = BALP isoforms treated with neuraminidase.

Article Snippet: We thank Philippe Crine at Enobia Pharma for the generous contribution of the recombinant BALP isoform sALP-FcD 10 .

Techniques: Activity Assay

Journal:

Article Title: Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms

doi: 10.1016/j.bone.2009.07.009

Figure Lengend Snippet: Migration of BALP isoforms in a native gel. B1, B2, B1x and B/I are untreated BALP isoforms and B1*, B2*, B1x* and B/I* are isoforms treated with neuraminidase prior analysis. The untreated isoforms had different migration patterns through the gel, but more similar migration patterns after treatment with neuraminidase.

Article Snippet: We thank Philippe Crine at Enobia Pharma for the generous contribution of the recombinant BALP isoform sALP-FcD 10 .

Techniques: Migration

Journal:

Article Title: Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms

doi: 10.1016/j.bone.2009.07.009

Figure Lengend Snippet: Specific binding of different lectins to denatured BALP isoforms in order to characterize different patterns of glycosylation

Article Snippet: We thank Philippe Crine at Enobia Pharma for the generous contribution of the recombinant BALP isoform sALP-FcD 10 .

Techniques: Binding Assay, Glycoproteomics

Journal:

Article Title: Glycosylation differences contribute to distinct catalytic properties among bone alkaline phosphatase isoforms

doi: 10.1016/j.bone.2009.07.009

Figure Lengend Snippet: Dose-dependent lectin precipitation on native BALP isoforms: B1 (●), B2 (○), B1x (▼;), and B/I (△). Each data point is expressed as a mean of samples in duplicate. (A) DSA, 0–5 mg/mL; (B) DSA, 0–0.5 mg/mL; (C) SNA, 0–5 mg/mL; and (D) PNA, 0–5 mg/mL. DSA caused significant precipitation, even at low concentrations, for all four BALP isoforms, whereas no major precipitation was observed for SNA and PNA.

Article Snippet: We thank Philippe Crine at Enobia Pharma for the generous contribution of the recombinant BALP isoform sALP-FcD 10 .

Techniques: