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Biomedical subjects

D A Ledward

Publications and source records attributed to D A Ledward.

11 recordsLinked to original sources
PubMed1989

Effects of dietary iron deficiency and tungsten supplementation on 59Fe absorption and gastric retention from 59Fe compounds in rats.

1. In vivo 59Fe absorption from intrinsically labelled Fe-containing fractions of liver and blood were measured in rats by intragastric dosing. All rats were fed on a low-Fe diet for 3 d before dosing in order to standardize the Fe status of the intestinal mucosal cells. 2. An increase in digestion time from 2 to 12 h increased 59Fe absorption (P less than 0.01) from all fractions except ferritin. 3. Fe-deficient rats when compared with essentially Fe-replete rats showed decreased gastric retention for all fractions, but increased 59Fe absorption over 2 h only from ferritin. Ferritin showed several unusual absorption characteristics. 4. Dietary tungsten supplementation of Fe-deficient rats reduced the ferroxidase activity of intestinal mucosal xanthine oxidase. In addition, gastric retention and 59Fe absorption (P less than 0.05) from all fractions were increased.

Animals↗
PubMed1978

Iron availability from meat.

1. The distribution of radioactive iron in 59Fe-labelled rat muscle extract was determined using gel filtration. This showed that most (approximately 70%) of the radioactivity was associated with the heamatin compounds; myoglobin and haemoglobin. 2. Raw beef and freeze-dried rat muscle were digested in vitro, under simulated physiological conditions, and after centrifugation the supernatants fractionated by gel filtration. The soluble products were haematin Fe complexes of molecular weight above 10,000 and non-haematin Fe compounds of molecular weight below 6000, the major products being the non-haematin Fe complexes. The soluble compounds were also separated by dialysis and, in rat muscle, it was found that the low-molecular-weight non-haematin compounds accounted for more than 80% of the total soluble iron. 3. In vivo absorption studies with rats showed the Fe in a digested muscle dialysate to be more readily absorbed than that from an aqueous muscle extract which itself was more readily absorbed than the Fe from whole blood. 4. It may not, therefore, be the haemoproteins per se which are responsible for the high availability of Fe in meat, but rather the nature of their degradation products, formed by digestion within the meat environment.

Animals↗
PubMed1978

Protein quality and iron availability of intermediate moisture beef stored at 38 degrees C.

The longissimus dorsi of a bull and steer were cut into cubes 1.5 cm3 and processed to a water activity (aw) 0.85 by canning in a solution of 9.5 p. 100 sodium chloride, 0.5 p. 100 potassium sorbate and a pre-determined amount of glycerol and water for sixteen hours with continuous tumbling on an end over shaker. After partial drying the intermediate moisture (i.m.) meat pieces were stored at 38 degrees C for periods up to 24 weeks and then freeze-dried before milling and incorporation into test diets fed to rats. Protein quality of fresh cooked beef and i.m. meat stored at 38 degrees C was measured in terms of net protein utilisation (NPU). There was no significant difference in NPU between cooked beef and freshly processed i.m. beef. There were no changes in NPU of i.m. meat from bull up to 9 weeks of storage. After 3 weeks of storage of the meat from the steer however, the NPU fell to 53.0, a level characteristic of cereal protein. This fall in NPU was associated with a decrease in the levels of all essential amino acids (in the protein hydrolysate). Valine and threonine being first and second limiting amino acids. Further storage of i.m. beef after 3 weeks produced a slower rate of decrease in NPU, the value at 24 weeks being 32.1 (61 p. 100 fall). Available lysine decreased by only 15 p. 100 after twenty-four weeks, this measurement under-estimating the fall in protein quality. The decrease in solubility of the meat in SDS/beta-mercaptoethanol on storage was of similar magnitude to that of NPU. Iron availability of i.m. meat, measured by haemoglobin regeneration in rats, showed improved iron availability compared to freshly cooked beef, even though marked changes had occurred in the meat heamatin complexes.

Animals↗
PubMed1976

Enthalphy changes associated with the denaturation of collagens of different imino acid content.

The enthalpy changes associated with the denaturation of acid-soluble and insoluble collagens prepared from sheep, cod, halibut and pike skin were determined by differential scanning calorimetry. The enthalpy change associated with the soluble collagens decreased with decreasing imino acid content (from 1420 cal/mol for sheep to 736 cal/mol for cod) while the value for insoluble collagens was approximately constant at 1360 cal/mol. A possible explanation for these values in terms of the nautre of the bonds present in collagen is discussed.

Collagen↗
PubMed1975

Structural and functional determinants of Mucor miehei protease. V. Enthalpy changes upon thermal denaturation in solution of varying pH.

The thermal denaturation of Mucor meihei protease was studied as a function of pH by differential scanning calorimetry. In both citric acid-Na2HPO4 and in acetic acid-sodium acetate buffers, maximum thermal stability was at pH 4.0-4.2. However, the maximum enthalpy changes associated with the denaturation process were buffer-dependent and occurred between pH values of 4.7 and 5.7.

Calorimetry↗
PubMed1970

Hydrogen sulfide production by bacteria and sulfmyoglobin formation in prepacked chilled beef.

Meat stored at 1 to 2 C under low oxygen tensions, either in gas-impermeable packs or in controlled atmospheres, occasionally exhibited an undesirable green exudate. The green pigment was identified spectrophotometrically as sulfmyoglobin. The conversion of myoglobin to sulfmyoglobin resulted from the production of H(2)S by bacteria tentatively identified as Pseudomonas mephitica. This organism produced H(2)S only when the oxygen tension was about 1% and the pH of the meat was 6.0 and above.

Animals↗
PubMedDate not supplied

Stability of sorbic acid in intermediate moisture systems.

Intermediate foods are a heterogeneous group of foods which are stabilized by lowering their water activity to a level insufficient to support bacterial growth, typically about 0.85. However, moulds and yeasts are able to grow at these water activities and it is usual to add an antimycotic such as sorbate to ensure microbial stability. Sorbate, though, is liable to oxidation and in model systems adjusted to a water activity of 0.85 some of the oxidation products were found to be potential reactants in non-enzymic browning reactions with lysine, glutamate and haemoglobin solutions when stored at 38 degrees C or 65 degrees C. Oxidation led to an increase in pH and the formation of thiobarbituric acid-reactive substances. In some intermediate moisture meat products prepared by cook-soak equilibration in a variety of humectant solutions, 0.3% sorbate induced the formation of covalent linkages between proteins on storage at 38 degrees C. The concentration of sorbate in the meats decreased by a factor of 2 during 4 months at this temperature. The effects of such reactions on the quality of the food are discussed.

Drug Stability↗