Apparent total tract macronutrient digestibility, fecal characteristics, and fecal fermentative end-product concentrations of healthy adult dogs fed bioprocessed soy protein.

Animal proteins are commonly used in extruded dog foods. Plant-based proteins have a more consistent nutrient profile than animal sources but may contain antinutritional factors, including trypsin inhibitors and oligosaccharides. Bioprocessed soy protein (SP; HP-300; Hamlet Protein, Inc., Findlay, OH) is a processed soy-based product with low antinutritional factor concentrations and high protein quality. The objective was to evaluate the effects of SP on apparent total tract macronutrient digestibility, fecal characteristics, and fecal fermentative end products. Furthermore, this study aimed to identify if SP can be a replacement for poultry byproduct meal (PBPM) in dog food and determine if there are practical limits to its use. Three palatability experiments were conducted to evaluate 1) 0 vs. 12% SP, 2) 0 vs. 48% SP, and 3) 12 vs. 48% SP. For digestibility, 48 healthy adult Beagle dogs (20 females and 28 males; 3.4 yr mean age and 10.0 kg mean BW) were randomly allotted to 1 of 6 dietary treatments, 0 (control), 4, 8, 12, 24, and 48% SP, in a completely randomized design. All diets were formulated to meet Association of American Feed Control Officials nutrient profiles and contained approximately 30% CP and 16% fat. The treatment period consisted of a 10-d diet adaptation phase followed by a 4-d fresh and total fecal collection phase. The palatability results suggest that of the 3 inclusion levels tested (0, 12, or 48% SP), the best inclusion of SP is 12%, which was preferred over 0 and 48% SP. Digestibility and fecal data were evaluated for linear and quadratic effects using SAS. Stool output (on both an as-is and a DM basis) did not differ from the control except for the 48% SP treatment ( < 0.01). Fecal output per unit food intake differed ( < 0.01) from the control only at the 24 and 48% SP inclusion rates. No significant effects of feeding SP were found on stool consistency scores. Digestibility of DM, OM, and energy did not differ from the control at any inclusion rate, except for a decrease ( < 0.01) at 48% SP. Apparent total tract CP digestibility was not affected by treatment and ranged from 82.9 to 86.2%. Fecal short-chain fatty acid concentrations were greater ( < 0.01) in dogs fed 24 and 48% SP compared with the control. Conversely, branched-chain fatty acid concentrations were lower ( < 0.01) in dogs fed 8 to 48% SP compared with the control. These data suggest that SP is a suitable replacement for PBPM in dog diets up to a 24% inclusion level.

Influence of dry heat treatment and anticoagulant on coupling of fibrinogen and fibronectin to von Willebrand factor in normal plasma.

In plasma from healthy subjects a coupling was identified between von Willebrand factor (vWf), fibrinogen (fg), and fibronectin (fn) that was dependent of anticoagulants heparin, EDTA, and citrate. Binding was quantitated by ELISA methodologies, based on polyclonal antibodies directed against the proteins studied, in order to express the percentage of moles of fg or fn bound to moles vWf, C[fg/vWf] or C[fn/vWf] (mol/mol)%. The intra-assay coefficients of variation (CV%) for fg and fn bound to vWf were 10.6% and 7.4% (n = 10) respectively, and the inter-assay coefficients of variation were 24.4% and 22.2% (n = 10). The largest degree of coupling was found in heat-treated lyophilized heparin plasma, where C[fg/vWf] and C[fn/vWf] were 12.9 +/- 1.4 (mol/mol)% and 2.4 +/- 0.1 (mol/mol)% (mean +/- SD). Binding was further qualitatively demonstrated through experiments using gel filtration chromatography and agarose gel electrophoresis followed by immunoblotting. In all instances coupling of vWf with fg was higher than with fn. Lyophilisates of normal plasma that were subjected to dry heating (60 degrees C in 72 h) showed considerably increased coupling. Previous investigators, studying reconstituted factor VIII concentrates by means of gel filtration, pointed out that an association between vWf, fg and fn was present in such therapeutic material. This investigation signifies that a coupling between these proteins may be present even in the source plasma, and that 'dry heating' increases binding. Implications of these results are discussed.