Test instrumentation evaluates electrostatic hazards in fluid system

RJ-1 fuel surface potential is measured with a probe to determine the degree of hazard originating from static electricity buildup in the hydraulic fluid. The probe is mounted in contact with the fluid surface and connected to an electrostatic voltmeter

The Soil Conversation Experimental Farm

In its 35-year life, the Soil Conservation Experimental Farm in Page County has provided information on water runoff, soil loss, erosion control, and watershed management and production problems of beef cow herds

SOIL QUALITY ATTRIBUTE TIME PATHS: OPTIMAL LEVELS AND VALUES

We develop a dynamic soil quality model to evaluate optimal cropping systems in the northern Great Plains. Modeling soil quality attributes is feasible, and attribute model results apply to a wide range of soils. A crop production system with continuous spring wheat and direct planting is the most profitable system. This system has low soil erosion and high quality attributes, indicating the benefits of increased soil quality exceed the higher maintenance costs. On-site value of additional soil organic carbon (OC) ranges from $1 to$4/ton OC/hectare/year. These values for soil OC impact the optimum tillage practice, but not the crop rotation.Crop Production/Industries,

Incorporation in vitro of labeled amino acids into bone marrow cell proteins

Nearly all experiments on the incorporation of labeled amino acids into tissue proteins in vitro have been done on tissues whose cell structure has been partially or completely disintegrated, e.g. tissue slices, segments, or homogenates. Since cell destruction reduces or abolishes the uptake of labeled amino acids (1), it seemed worth while to carry out studies on intact cells in vitro. Bone marrow cells were found to be suitable for this purpose. The labeled amino acids used were glycine-1-C14, L-leucine-1-C14, L-lysine-1-C14, and L-lysine-6-C14

Isolation of a peptide in guinea pig liver homogenate and its turnover of leucine

Leucine was synthesized with C14 in the carboxyl group. 10 mg. of the radioactive amino acid (DL) and 0.66 gm. (wet weight) of guinea pig liver homogenate were added to a reaction mixture containing 1.3 per cent of an amino acid mixture corresponding to the composition of casein and 0.005 M fumarate, all in a final volume of 4 ml. of isotonic saline solution(1) at pH 7.4. The reaction was carried out under oxygen for 6 hours at 38°

The incorporation of labeled lysine into the proteins of guinea pig liver homogenate

When C14-labeled lysine is incubated with guinea pig liver homogenate, α-aminoadipic, α-ketoadipic, and glutaric acids are formed from the lysine (1). These transformations were established by finding the radioactivity of the C14 tracer in the metabolic products. The homogenate proteins coagulated by boiling at pH 5 also contained radioactivity. The counts given by the proteins corresponded to about 0.02 to 0.03 per cent of that added as lysine; the extent of lysine incorporation into the proteins was of the same order of magnitude as Melchior and Tarver (2) had found after incubating S35-labeled methionine and Winnick et al. (3, 4) C14-labeled glycine with rat tissue homogenates. Yet we could not satisfy ourselves that the radioactivity remaining in the proteins in our experiments, although it persisted through exhaustive extraction, did not come from traces of adsorbed radioactive lysine. Some counts were found in the protein when the homogenate was boiled prior to incubation with isotopic lysine

Alpha-aminoadipic acid: A product of lysine metabolism

As part of a study of protein and peptide metabolism lysine was synthesized with C14 in the ε position and resolved into the L and D isomers. 10 mg. of labeled lysine dihydrochloride (either L- or D-) and 0.66 gm. (wet weight) of guinea pig liver homogenate were added to a reaction mixture containing 1.3 per cent of an amino acid mixture corresponding to the composition of casein except for lysine and 0.01 M α-ketoglutarate, all in a final volume of 4 ml. of isotonic saline solution.(1) The reaction was carried out under oxygen for 6 hours at 38°

Incorporation in vitro of labeled amino acids into proteins of rabbit reticuloytes

Continuing our work on the incorporation of labeled amino acids into proteins (1), we have begun a study of the incorporation in vitro of C14-labeled glycine, L-histidine, L-leucine, and L-lysine into the proteins of rabbit reticulocytes. In preliminary experiments the incorporation into the hemoglobin isolated from the reticulocytes was determined. But, after it was found that plasma contains factors accelerating amino acid incorporation, it was decided to proceed as rapidly as possible toward the identification of these factors; we have, therefore, measured incorporation into the total proteins of the reticulocytes, since isolation of the hemoglobin was time-consuming. The results obtained with hemoglobin and with the total proteins are essentially the same, indicating that the other proteins of the reticulocytes incorporate amino acids at approximately the same rate as hemoglobin