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Biomedical subjects

R L Preston

Publications and source records attributed to R L Preston.

At least 55 records · Page 3Linked to original sources
PubMed1980

Effect of avoparcin and monensin on performance of finishing heifers.

One-hundred and fifty crossbred yearling-heifers, averaging 264 +/- 17 kg were fed a 77% barley diet for 140 days to evaluate the effect of 0, 33, 49.5 and 66 ppm avoparcin and 33 ppm monensin on growth rate, feed efficiency, carcass quality and ruminal volatile fatty acid (VFA) concentration. Heifers were allotted by weight to 25 pens (six head per pen) in a randomized complete block design of five treatments and five replicates per treatment. On day 140, rumen fluid was obtained from a randomly selected replicate of six heifers from each treatment for VFA analysis. Carcass data and liver samples were obtained at slaughter on day 147. All avoparcin-fed cattle consumed less feed per unit gain (P less than .05) than did those in the control group. Feed intakes of the monensin-fed heifers and the heifers fed 49.5 ppm avoparcin were lower (P less than .05) than those of the control group. There were no differences (P greater than .05) between treatments for measured carcass, liver or rumen parameters.

Animals↗
PubMed1975

Utilization of nitrogen from soybean meal, casein, zein, and urea by mature sheep.

The utilization of nitrogen contained in soybean meal, casein, zein, and urea was studied in 12 mature wethers. Net microbial synthesis rates during the 6-hour period after feeding corresponded to ruminal ammonia concentrations, suggesting that the ruminal ammonia level in these experiments was a limiting factor in microbiol protein synthesis. Maximum conversion of dietary nitrogen to microbial nitrogen in the rumen during a 24-hour period was estimated to be 62.5, 85.3, 40.9, and 90.1%, respectively, for soybean meal, casein, zein, and urea. Estimated production rates of acetic, propionic, butyric, isovaleric, and valeric acids during the first 6 hours after feeding suggested that zein supported the lowest microbial activity in the rumen, and that urea supplementation resulted in isovaleric and valeric acids production rates equivalent to or greater than rates when the other nitrogen supplements were present in the diet. Daily endogenous urinary and metabolic fecal nitrogen determined by regression analysis utilizing soybean meal as the only nitrogen supplement were 72 mg/kg body weight0.75 and 340 mg/100 g of dry matter intake. Biological values of 84.8, 78.3, 84.3, and 76.4 were obtained for soybean meal, casein, zein, and urea, respectively.

Animal Feed↗
PubMed1975

Comparative response of castrate and intact male rats to diethylstilbestrol.

Treatment of castrate and intact male rats with DES in the feed was used to note its comparative effect on feed intake vesicle, testicle, spleen and liver weights, and DES similarly reduced gain and feed efficiently in both castrate and intact male rats. Thus, there appears to be a basic difference in the response of rats to DES, compared to cattle and sheep, that does not depend on whether they are intact or castrate males.

Animals↗
PubMed1974

Structure-affinity relationships of substrates for the neutral amino acid transport system in rabbit ileum.

The apparent affinities of various amino acids for the neutral amino acid transport system in rabbit ileum were determined by measuring the inhibition of L-methionine-(14)C influx across the brush border membrane. The apparent affinity was very low for compounds lacking an alpha-amino group, compounds with the alpha-hydrogen substituted by a methyl group, D-compounds, compounds with tertiary branching in the side chain, compounds with either a positive or negative charge in the side chain, and in most cases, compounds with a hydrophilic moiety in the side chain. High apparent affinities were exhibited by compounds with unbranched carbon or carbon-sulfur side chains. Branched compounds such as valine and leucine exhibited affinities which correlate with binding of only the linear portion of the side chain. The calculated change in free energy of binding is 370 cal/mol/CH(2) group which suggests the binding region for the side chain is partially hydrophobic. The affinities of families of analogues, derivatives of cysteine, methionine, serine, alanine, valine, and phenylalanine, correlate with their calculated octanol/water partition coefficients and are also correlated with apparent structural and electronic differences between families. The data permit a preliminary description of the functional geometry of the neutral amino acid transport site. The site contains a region for binding the alpha-amino group, alpha-carboxyl group, and side chain. The regions about the alpha-amino group and alpha-hydrogen are quite sterically limited. The side chain binding region is hydrophobic in nature and appears to be shallow, binding only the linear portion of branched or ring compounds.

Amino Acids↗
PubMed1973

Inhibition of amino acid transport in rabbit intestine by p-chloromercuriphenyl sulfonic acid.

Influx of phenylalanine across the brush border of rabbit intestine is markedly reduced by treatment with 5 mM p-chloromercuriphenyl sulfonate (PCMBS). The effect is rapidly and completely reversed by dithiothreitol. Phenylalanine influx into PCMBS-treated tissue can be competitively inhibited by other neutral amino acids and follows saturation kinetics. PCMBS causes an increase in the apparent Michaelis constant from the value observed in control tissue but does not alter the maximal influx significantly. Treatment of the tissue with PCMBS leads to a significant reduction in the Na-sensitivity of the transport, and a number of results indicate that the major effect of the reagent is to cause a marked reduction in the affinity of the transport system for Na. The transport system can be partially protected against reaction with PCMBS by phenylalanine and tryptophan but not by methionine or norleucine. The results suggest that PCMBS reacts with a sulfhydryl group in the region of the transport site and may alter conformational changes associated with the binding of substrates.

Amino Acids↗