Fourier-transform spectroscopy and global deperturbation treatment of the A1Σu+ and b3Πu states of K2 in the entire bound energy range.

Rotationally resolved Fourier-transform spectra of laser-induced fluorescence A1Σu+∼b3Πu→X1Σg+ of K2 molecules were recorded and analyzed, yielding 4053 term values of the spin-orbit (SO) coupled A ∼ b complex of the 39K2 isotopologue with ∼0.01 cm-1 accuracy. Their compilation with 1739 term values from previously published sources allowed them to cover the energy range [9955, 17 436] cm-1 from the bottom of the lower-lying b3Πu state up to the vicinity of the atomic asymptote 4s2S12 + 4p2P12, with a rotational quantum number J ∈ [0, 149]. The experimental data were processed by a direct 6 × 6 coupled-channel (CC) deperturbation treatment, which accounted explicitly for both SO and electronic-rotational interactions between all six e-symmetry states: A1Σu+(0u+), b3Πu(0u+,1u,2u), c3Σu(1u), and B1Πu(1u). The initial parameters of the global deperturbation model have been estimated in the framework of ab initio electronic structure calculations applying multi-reference configuration-interaction and coupled-clusters methods. The interatomic potentials analytically defined for A and b states, as well as SO-splitting of the triplet b state and A ∼ b SO-coupling functions, have been particularly refined to fit the 5792 term values of the 39K2 isotopologue, whereas the rest parameters were fixed on their ab initio values. The resulting mass-invariant parameters of the 6 × 6 CC model reproduced the overall rovibronic term energies of the A ∼ b complex of 39K2 with accuracy, which is well within the experimental errors. The quality of the deperturbation analysis was independently confirmed by comparison with the present obtained 705 and 14 term values of respective 39K41K and 41K2 isotopologues, as well as by agreement between measured and predicted relative intensity distributions in long A ∼ b → X(vX) band progressions. This deperturbation analysis provided the refined dissociation energy Tdis = 17 474.569(5) cm-1 and the long-range coefficient C3Σ = 5.501(4) × 105 cm-1 Å3 relevant to the non-relativistic atomic limit 4s + 4p. The derived Tdis yielded the accurate well depth De = 4450.910(5) cm-1 for the ground X1Σg+ state, whereas the new C3Σ value yielded the improved estimates for atomic K(4p2P12;32) radiative lifetimes, τ12 = 26.67(3) and τ32 = 26.32(3) ns.

Sources of variation in rates of in vitro ruminal protein degradation.

Rates and extents of ruminal protein degradation for casein, solvent soybean meal (SSBM), expeller soybean meal (ESBM), and alfalfa hay were estimated from net appearance of NH3 and total amino acids in in vitro media containing 1 mM hydrazine and 30 mg/L of chloramphenicol. Protein was added at 0.13 mg of N/mL of medium, and incubations were conducted for 4 to 6 h, usually with hourly sampling. Inocula were obtained from ruminally cannulated donor cows fed diets of grass silage or alfalfa and corn silages plus concentrates. Preincubation or dialysis of inocula was used to suppress background NH3 and total amino acids; however, preincubation yielded more rapid degradation rates for casein and SSBM and was used in subsequent incubations. Preincubation with added vitamins, VFA, hemin, or N did not alter protein degradation. Protein degradation rates estimated for SSBM, ESBM, and alfalfa were not different when computed from total N release or N release in NH3 plus total amino acids, regardless of whether amino acids were quantified using ninhydrin colorimetry or o-phthalaldehyde fluorescence. Accounting for the release of peptide-N also did not affect estimated degradation. However, casein degradation rates were more rapid when using total N release or accounting for peptide-N, indicating significant accumulation of small peptides during its breakdown. Rates also were more rapid with inocula from lactating cows versus nonlactating cows with lower feed intake. Protein degradation rates were different due to time after feeding: casein rate was more rapid, but SSBM and ESBM rates were slower with inocula obtained after feeding. Several characteristics of ruminal inoculum that influenced breakdown of the rapidly degraded protein casein did not appear to have direct effects on degradation of protein in soybean meal.