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Biomedical subjects

K N Boorman

Publications and source records attributed to K N Boorman.

At least 19 recordsLinked to original sources

Dietary phosphorus supply, egg-shell deposition and plasma inorganic phosphorus in laying hens.

1. In 2 experiments the effects of dietary phosphorus on relationships between plasma inorganic phosphorus concentration (Pi), shell and egg production and depletion states were measured in brown laying hens. 2. In a 12-week experiment dietary phosphorus concentrations from conventionally deficient (1.6 g non-phytate-phosphorus (PNP)/kg) to moderate excess (3.9 g PNP/kg) had little effect on egg and shell production, although there was evidence that plasma Pi concentration, when not influenced strongly by shell formation, reflected dietary phosphorus content. 3. Among birds at each dietary phosphorus concentration there was a negative linear relationship between shell weight of early eggs in the sequence and plasma Pi concentration. The relationship was apparently not affected by dietary phosphorus concentration. 4. Continued feeding of the deficient diet to 61 weeks of age did not have effects on body weight, egg and shell production, other than those associated with age, but plasma Pi and bone measurements indicated marginal phosphorus depletion. 5. In another experiment excessive dietary phosphorus (11.9 g PNP/kg) fed in a cross-over design caused small adverse effects on shell production, increased food intake and body weight and increased plasma Pi content, while there was no relationship between shell weight and plasma Pi concentration. 6. The results are consistent with an indirect effect of plasma phosphorus accumulation on shell formation, probably via an inhibitory effect on skeletal calcium release, in addition to any effect of excess dietary phosphorus on intestinal calcium availability. 7. Phosphorus requirement and status in the laying hen are complicated by the failure to recognise the contribution of digestible phytate-phosphorus to the available phosphorus supply.

Animal Feed↗

Ubiquitin gene expression and ubiquitin conjugation in chicken muscle do not reflect differences in growth rate between broiler and layer birds.

Previous work has shown that chicken strains selected for growth (broilers) degrade muscle proteins less rapidly than those selected for egg laying. They also have decreased calpain and increased calpastatin content in breast muscle. This study aimed to test the hypothesis that these differences correlate with changes in the ATP- and ubiquitin-dependent proteolytic system. Chickens of a broiler strain (Ross 1) and a layer strain (ISABrown) were reared to the age of 4 wk under identical conditions with ad libitum access to feed and water. Mean fractional growth rates were 10.4%/d for broilers and 7.4%/d for layers. Feed intake measured in the last week of the trial was slightly greater in layer birds (.11 and .12 g x g body weight(-1) x d(-1) for broilers and layers respectively; P < .006). Polyubiquitin (UbI) messenger RNA was abundant in the muscles of these well-fed birds, but it showed little difference between strains. Muscle did not significantly express the UbII polyubiquitin gene. The ATP-dependent system conjugating ubiquitin to endogenous proteins had greatest activity in the gastrocnemius muscle of broiler birds but was not significantly different between breeds. Proteins cross-reactive with antisera to recombinant human proteasome regulatory subunits MSS1 (multicopy suppressor of SUG 1; S7) and TBP1 (tat binding protein 1; S6') were present in muscle homogenates from both strains of bird. The chick equivalent of TBP1 was more abundant in breast muscle of broiler birds than in leg muscle, or in either muscle of layers. Antiserum to recombinant yeast subunit mts2 (mitosis temperature sensitive gene 2; S4) did not react with any protein of the expected size but detected a 30-kDa peptide that was not associated with the 26S proteasome; this was found only in muscle from the layer strain. Hence, during normal growth of chickens, rates of protein degradation are not controlled by the expression of ubiquitin mRNA or the conjugation of ubiquitin. However, the composition of the 26S proteasome may be a regulatory factor.

ATPases Associated with Diverse Cellular Activitie↗

Maximum nutritional response to poor-quality protein and amino acid utilisation.

1. Although the theory of responses to amino acids suggests that, providing sufficient of the limiting amino acid is fed, it should be possible to elicit maximum growth response, maximum response is not usually elicited by poor quality proteins. 2. It has been suggested that this failure to elicit maximum response is a reflection of poorer limiting amino acid utilisation from poor-quality proteins. This interpretation conflicts with the theory of general amino acid imbalance which proposes that amino acid excesses do not impair the utilisation of the limiting amino acid. 3. Three protein mixtures of different quality were made by mixing maize gluten meal and soyabean protein concentrate in constant proportions, supplementing with tryptophan, threonine and arginine to adequacy and varying amino acid score (0.62, 0.71 or approximately 10) by varying additions of free lysine. The 3 mixtures were diluted with protein-free ingredients to produce 3 diet series, each providing 3.7, 6.5, 9.2, l2.0, 14.8 and 17.5 g lysine per kg. Each diet was fed to 4 cages of 2 chickens each from 4 to 14 d of age in a randomised block experiment. Food intake, body-weight and body-nitrogen gain were measured. 4. Differences in protein quality were confirmed by regression analyses of bodyweight response to protein intake (Net Protein Ratio) and body-nitrogen response to nitrogen intake (Net Protein Utilisation) in the linear range. Regression analyses in the linear range of body-weight or body-nitrogen response to lysine intake showed no adverse effect of protein quality on lysine utilisation. Curvilinear analysis (Reading flock response model) confirmed this finding. 5. Maximum response could not be obtained with the poorest protein quality. It is illogical to invoke impaired utilisation of the limiting amino acid to explain this. A small decrease in net energy yield of the diet may be sufficient to explain the effect, but it is more likely that the depletion of the limiting amino acid from tissue (muscle) protein which results from feeding poor-quality protein explains the effect.

Amino Acids↗

Egg-shell deposition and blood plasma inorganic phosphorus concentration in individual laying hens.

1. The relationship between plasma inorganic phosphorus measured at the end of the dark period and the weight of the next egg shell produced was investigated in 30 Hisex Brown hens. 2. Hens received an adequate conventional layers' diet and the lighting pattern was conventional (17 L: 7 D). Observations were made early (31 to 40 weeks) and late (62 to 68 weeks of age) in the laying period. 3. Eggs were classified by position in the clutch sequence and significant negative correlations were found between shell weights of early eggs in the sequence and plasma phosphate at the end of the dark period. 4. No significant trends were found in plasma total calcium. 5. No significant differences were found in bone compositions of birds producing consistently more or less than average shell weight during the laying period. 6. The negative correlations between plasma phosphate and shell weight are consistent with the observations of Sauveur and Mongin (1983) and show that impairment of shell deposition is associated with skeletal mobilisation as indicated by increase in plasma phosphate. This is consistent with the observations on bone composition and indicates that selection for shell quality will tend to select birds which are not dependent on excessive skeletal mobilisation during shell formation.

Analysis of Variance↗

Protein synthesis in isolated perfused rat skeletal muscle. Contribution of intra- and extracellular amino acid pools.

Protein synthesis was measured in perfused rat skeletal muscle using [14C]lysine in the presence of increasing amounts of lysine in the perfusate. The results obtained clearly indicated that both the extracellular and intracellular pools of amino acids act as direct precursors for protein synthesis and analysis of the data, according to O'Hara et al. (J. molec. cell. Cardiol. 13, 925-940, 1981) further indicated that extracellular sources of lysine supplied 64 and 81% of the lysine incorporated in the absence and presence of insulin, respectively. The rate of protein synthesis were assessed to be 0.22 mumol lysine incorporated g-1 muscle per 3 hr of perfusion increasing to 1.0 mumol g-1 3 hr-1 in the presence of insulin.

Amino Acids↗

Amino acid supply and protein metabolism in isolated perfused rat skeletal muscle.

The uptake of amino acids by the perfused rat hind-limb at increasing perfusate amino acid concentrations was studied both in the presence and absence of insulin. The uptake of the essential amino acids could be correlated with their concentrations in muscle protein. A net protein synthetic rate was calculated from the predicted incorporation of phenylalanine and was 33 nmol h-1g-1, a value in good agreement with those obtained in other studies. The possible significance of the supply of leucine in the regulation of muscle protein synthesis is considered.

Amino Acids↗

Carotid or jugular amino acid infusions and food intake in the cockerel.

1. Infusions of histidine into the carotid arteries of cockerels receiving a histidine-limiting, imbalanced diet caused an increase in food intake, whereas similar infusions into the jugular veins did not. 2. Infusions of lysine into the carotid arteries or jugular veins of young cockerels receiving a balanced, low-protein diet caused decreases in food intake. There was evidence of a more marked effect of carotid infusion. 3. The mechanisms of food intake regulation by amino acids in mammals are applicable to birds and excesses of single amino acids do seem to affect food intake directly.

Animals↗

Nitrogen retention in the pig.

I. Published results have been used to study the relationships between nitrogen retention (NR), body-weight (W) and N intake in the pig. 2. The general decrease in maximal NR (g/d per kg W0.75) with increasing W (kg) was curvilinear for values of W from 1-5 to 45: NR = 3.324--0.098 W + 0.001 W2; and rectilinear for values of W from 45 to 165: NR = 1.252--0.006 W. Values for protein requirements derived from these equations agreed closely with published estimates. 3. The slopes of the curves for NR (g/d per kg W0.75) v. N intake (g/d) decreased as W (kg) increased from about 2.5 to 190. After extrapolation to a proposed common intercept on the NR axis of--150 mg N/d per kg W0.75, regression analysis of the intercepts of these curves on the N-intake axis v. W gave an estimate of N requirements for maintenance of 246 + 19 mg/d per kg W0.75. 4. The results also indicated that at low N intakes net protein utilization (N retention + total obligatory N losses divided by N intake) was essentially independent of W, whereas the gross efficiency of N utilization (NR divided by N intake) was influenced by both W and N intake.

Animals↗

Urate synthesis in the perfused chick liver.

Urate synthesis was studied in a perfused chicken liver preparation. The perfused liver had an ATP/ADP ratio of 0.29+/-0.05(6) compared with 0.34+/-0.07(10) in liver obtained from chicks under ether anaesthesia. Lactate/pyruvate ratios were 9.4+/-1.7(5) in the perfused liver and 14.8+/-1.8(5) in the rapidly sampled liver. Urate synthesis was only marginally stimulated by glycine, glutamine, aspartic acid or NH(4)Cl, but significant increases were observed with phosphoribosyl pyrophosphate, aminoimidazolecarboxylic acid riboside, inosine, inosinic acid and xanthine. Urate synthesis from glycine, glutamine, NH(4)Cl, asparagine, alanine, histidine and a mixture of 21 amino acids was obtained on inclusion of insulin in the perfusion medium. Evidence for the inclusion of the carbon of histidine into uric acid was obtained. Aspects of the energy consumption associated with the conversion of excess of amino acid into uric acid are considered.

Adenosine Diphosphate↗