Optimization of rate and efficiency of dietary nitrogen utilization through the use of animal by-products and(or) urea and their effects on nutrient digestion in Holstein steers.

The objective of this N balance study was to determine the potential for improving the efficiency and rate of dietary N utilization in Holstein steers by feeding an amino acid-balanced mixture of animal by-product protein sources in combination with urea. The Beef NRC 1996 Model Level 2 was used to formulate a corn-based (86:14 concentrate-hay) control diet with soybean meal as the primary N supplement that would provide ME and metabolizable protein (MP) allowable ADG of 1.4 kg in 250-kg steers with an estrogenic implant and fed an ionophore. A combination of porcine meat and bone meal, fish meal, hydrolyzed feather meal, and blood meal was also formulated as an undegradable intake protein (UIP) blend to complement those amino acids (AA) derived from microbial protein synthesis. Four steers with an average initial BW of 259 kg were assigned in a 4 x 4 Latin square design to treatments consisting of control, two levels of UIP inclusion (2.6 and 5.2%; DM basis) in combination with urea, and a negative control "urea diet" containing no UIP and no SBM. The steers were fed at hourly intervals 95% of ad libitum intake and were injected with 500 microg of estradiol-17beta twice daily. Nitrogen intakes were 155, 160, 162, and 145 g/d, and N balances were 47, 51, 42, and 47 g/d when the 0, 2.6, 5.2% UIP and the urea diets were fed, respectively. Nitrogen balance was reduced with the 5.2% UIP diet (P < 0.05), and was less than the capacity estimate derived from abosmasal casein infusion studies. Apparent N digestibilities averaged 69%, but DM, OM, and nonstructural carbohydrate digestibilities were significantly reduced for the urea diet. Feeding 5.2% UIP in the diet reduced (P < 0.05) the biological value from 46 to 38%, which was accompanied by a significant elevation of plasma urea N. Results indicate that genetic capacity for N retention was approximately 51 g/d. Results demonstrate that use of an AA-balanced blend of animal by-product protein sources did not improve the efficiency of dietary N usage when added to corn-based diets formulated with the Beef NRC 1996 Model Level 2 to meet nutrient requirements of rapidly growing steers. Using urea as the only N supplement achieved equal rate and efficiency of N use.

Changes in the calpains and calpastatin during postmortem storage of bovine muscle.

Changes in activity and protein status of micro-calpain, m-calpain, and calpastatin in bovine semimembranosus muscle during the first 7d of postmortem storage were monitored by using assays of proteolytic activity, SDS-polyacrylamide gel electrophoresis, and Western blot analysis. Extractable m-calpain activity changed slightly during the first 7d after death (decreased to 63% of at-death activity after 7d), whereas extractable calpastatin activity decreased substantially (to 60% of at-death activity after 1d and to 30% of at-death activity after 7d of postmortem storage) during this period. Extractable micro-calpain activity also decreased rapidly (to 20% of at-death activity at 1d and to less than 4% of its at-death activity at 7d after death) during postmortem storage. Western blot analysis showed that the 80-kDa subunit of m-calpain remained undegraded during the first 7d after death but that the 125- to 130-kDa calpastatin polypeptide was gone entirely at 7d after death. Hence, the calpastatin activity remaining at 7d originates from calpastatin polypeptides that are 42 kDa or smaller. The 80-kDa micro-calpain subunit was almost entirely in the 76-kDa autolyzed form at 7d after death; this form is proteolytically active in in vitro systems, and it is unclear why the postmortem, autolyzed micro-calpain is not active. Over 50% of total muscle micro-calpain is tightly bound to myofibrils 7d after death; this micro-calpain is also nearly inactive proteolytically. Unless postmortem muscle contains some factor that enables micro-calpain in this muscle to be proteolytically active, it is not clear whether micro-calpain could be responsible for any appreciable postmortem myofibrillar proteolysis.