Effects of Raw Pea Flour on Nutrient Digestibility and Immune Responses in the Preruminant Calf

Abstract

Two milk substitute diets for which the protein was provided either exclusively by skim milk powder (control) or partially (34%) by dehulled raw pea flour were given for 2 and 4 wk, respectively, to five preruminant calves, each fitted with a reentrant ileocecal cannula. Ileal apparent digestibility was lower with the pea diet during wk 1 than with the control diet. Four of the cannulated calves exhibited significant intolerance to the pea diet, resulting in lower digestibility during wk 4. In contrast, fecal digestibility of the pea diet, measured in four additional calves without reentrant cannulas, did not significantly decrease between wk 1 and 4. The AA composition of ileal digesta from the first group of calves did not vary greatly, suggesting that the differences observed in their apparent digestibility of proteins were due mainly to changes in the loss of endogenous proteins. However, pea legumin survived digestion in the small intestine in amounts generally equivalent to 1 to 3% of intake. Most of that undigested fraction was smaller than the native legumin: 40 to 200 kDa instead of 360 kDa. Also, a 45-kDa fragment was detected in the urine. Increased intestinal permeability could have favored the development of the high systemic anti-pea antibody titers that were observed in all of the calves.

Digestion of soybean globulins, glycinin, α-conglycinin and β-conglycinin in the preruminant and the ruminant calf

“…Proteins from feeds and digesta were extracted in borate buffer as described by Bush et al (1992). Immunometric ELISA's were set up for each purified soy globulin utilizing modifications of procedures described by Heppell (1985) and Heppell et al (1987 Values were expressed as native globulin equivalents.…”

“…The ELISA approach seems to be inappropriate for prediction of intestinal flow of dietarv oroteins in ruminants. Indeed, antibodiei riised against the native globulins cross-react with some but not all corresponding subunits (review by Brooks and Morr (1985)) and recognize fairly large globulin fractions in digesta (Bush et al 1992 (Spencer et al 1988) and to satisfactorily predict protein degradability (Romagnolo et al 1990 A possible contribution of the immune system to local (gut) unresponsiveness after weaning cannot be excluded.…”

“…They were then fitted with an abomasal catheter and an ileo-cecal re-entrant cannula under general anesthesia (Guilloteau et al 1986;Bush et al 1992 Brooks and Morr (1985) …”

Preparation of rabbit polyclonal antibodies against lupin storage proteins

“…Also, it has been shown that the B protein has negligible measurable sulfur amino acids, while the a protein contains less than I% and the 7 protein contains approximately 2% (Blagrove and Gillespie 1975). Doyle et al (1992) Bush et al (1992 (Towbin et al 1979). The lupin exffact was separated as before on a l% agarose gel and the proteins were ffansferred to nitrocellulose paper.…”

Digestibility, blood levels of nutrients and skin responses of calves fed soyabean and lupin proteins

“…Heated soyabean flour is the most widely used legume protein in monogastric feeding. However, it has been shown to cause immunological reactions in preruminant calves, which in severe cases can lead to alteration of the intestinal morphology of sensitized animals (Barratt et al, 1978;Kilshaw, 1981; Seegraber and Morrill, 1986 Bush et al, 1992). Thus the exploration of other temperate-growing legumes, such as lupins, becomes of interest particularly because of their high content of protein in the seed, which compares favorably with that of soyabean, and in some species is highest among legumes (Cerletti, 1993 (Hudson, 1979 (table I) and an 80% decrease in soluble sugars (data not shown), compared to those found in defatted soyabean (Lailbs et al, 1994) and lupin (Hudson, 1979;INRA, 1984) (Heppell et al, 1987) (Guilloteau et al, 1986).…”