scholarly journals Availability of iron from chicken meat and liver given to rats

1983 ◽  
Vol 50 (3) ◽  
pp. 511-520 ◽  
Author(s):  
Funke E. Bogunjoko ◽  
R. J. Neale ◽  
D. A. Ledward
Keyword(s):  
Gastrointestinal Tract ◽  
Time Course ◽  
Chelating Agents ◽  
Synergistic Effects ◽  
Gel Filtration ◽  
Chicken Meat ◽  
Soluble Extract ◽  
Breast Meat ◽  
Meat Extract ◽  
Stomach Emptying

1. The concentration and distribution of iron in 59Fe-labelled chicken leg and breast meat and liver were determined by gel filtration. In all samples approximately 50% of the Fe was insoluble (haemosiderin) and the haemoproteins (haemoglobin and myoglobin) constituted from 15% (liver) to 25% (leg meat) of the total Fe. Ferritin accounted for from 12% (leg meat) to 27% (liver) of the total Fe.2. A technique was developed which enabled the time-course of the passage of 59Fe-labelled whole and fractionated meat and liver through the gastrointestinal tract of Fe-replete and Fe-deficient rats to be followed and it was found that the rate of stomach emptying appeared to be a function of the viscosity of the meal. In Fe-replete rats approximately 71% of a meal of raw chicken meat had left the stomach within 1 h of administration and by 2 h the stomach was almost empty and much of the unabsorbed 59Fe was in the ileum. By 4 h the ileum and colon contained almost equal amounts of 59Fe. Between different test meals there were only slight differences in gastrointestinal distribution and these reflected the different rates of stomach emptying.3. Stomach emptying was slower in Fe-deficient compared with Fe-replete rats.4. In Fe-replete, but not Fe-deficient, rats it was found that the amount of 59Fe lost (absorbed) from the gastrointestinal tract 2 h after administration of a test meal was not significantly different from the value found using a 7 d faecal collection technique.5. Comparison of the 2 h absorption values for several test meals indicated that 59Fe absorption from raw whole meat was significantly higher than from the soluble extract and the residue after extraction (haemosiderin).6. Heat treatment caused a significant decrease in the absorption of Fe in whole meat and the soluble meat extract but a significant increase in the liver absorption values. It is suggested that denatured haemoproteins are less available for absorption than their native forms but that heating increases the availability of the Fe of haemosiderin or ferritin or both.7. Isolated muscle ferritin was poorly absorbed but on the addition of excess bovine serum albumin the absorption of the Fe was markedly increased.8. It is concluded that, to estimate the Fe availability of a food such as chicken meat or liver one must not only take account of the concentration and type of each Fe-containing compound present but also such factors as their possible synergistic effects, the presence of chelating agents, the extent of cooking and the concentration and type of proteinaceous digestion products.

scholarly journals Complexing of the CD-3 subunit by a monoclonal antibody activates a microtubule-associated protein 2 (MAP-2) serine kinase in Jurkat cells

1989 ◽  
Vol 262 (2) ◽  
pp. 449-456 ◽  
Author(s):  
C Hanekom ◽  
A Nel ◽  
C Gittinger ◽  
A Rheeder ◽  
G Landreth
Keyword(s):  
T Cells ◽  
Time Course ◽  
Gel Filtration ◽  
Maximal Activity ◽  
Jurkat Cells ◽  
Serine Kinase ◽  
Transient Activation ◽  
Normal Human ◽  
Dose Dependent

Treatment of Jurkat T-cells with anti-CD-3 monoclonal antibodies resulted in the rapid and transient activation of a serine kinase which utilized the microtubule-associated protein, MAP-2, as a substrate in vitro. The kinase was also activated on treatment of Jurkat cells with phytohaemagglutinin, but with a different time course. The activation of the MAP-2 kinase by anti-CD-3 antibodies was dose-dependent, with maximal activity observed at concentrations of greater than 500 ng/ml. Normal human E-rosette-positive T-cells also exhibited induction of MAP-2 kinase activity during anti-CD-3 treatment. The enzyme was optimally active in the presence of 2 mM-Mn2+; lower levels of activity were observed with Mg2+, even at concentrations up to 20 mM. The kinase was partially purified by passage over DE-52 Sephacel with the activity eluting as a single peak at 0.25 M-NaCl. The molecular mass was estimated to be 45 kDa by gel filtration. The activation of the MAP-2 kinase was probably due to phosphorylation of this enzyme as treatment with alkaline phosphatase diminished its activity. These data demonstrate that the stimulation of T-cells through the CD-3 complex results in the activation of a novel serine kinase which may be critically involved in signal transduction in these cells.

scholarly journals Role of Taste-Active Components, Glutamic Acid, 5'-lnosinic Acid and Potassium lon in Taste of Chicken Meat Extract

1996 ◽  
Vol 67 (5) ◽  
pp. 423-429 ◽  
Author(s):  
Shinobu FUJIMURA ◽  
Hidenori KOGA ◽  
Hiromi TAKEDA ◽  
Naoko TONE ◽  
Motoni KADOWAKI ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Chicken Meat ◽  
Active Components ◽  
Meat Extract

Thermal Inactivation of H5N1 High Pathogenicity Avian Influenza Virus in Naturally Infected Chicken Meat

2007 ◽  
Vol 70 (3) ◽  
pp. 674-680 ◽  
Author(s):  
COLLEEN THOMAS ◽  
DAVID E. SWAYNE
Keyword(s):  
Linear Regression ◽  
Avian Influenza ◽  
Thermal Inactivation ◽  
Chicken Meat ◽  
Meat Sample ◽  
Breast Meat ◽  
Infectious Dose ◽  
High Pathogenicity ◽  
Z Value ◽  
D Values

Thermal inactivation of the H5N1 high pathogenicity avian influenza (HPAI) virus strain A/chicken/Korea/ES/2003 (Korea/03) was quantitatively measured in thigh and breast meat harvested from infected chickens. The Korea/03 titers were recorded as the mean embryo infectious dose (EID50) and were 108.0 EID50/g in uncooked thigh samples and 107.5 EID50/g in uncooked breast samples. Survival curves were constructed for Korea/03 in chicken thigh and breast meat at 1°C intervals for temperatures of 57 to 61°C. Although some curves had a slightly biphasic shape, a linear model provided a fair-to-good fit at all temperatures, with R2 values of 0.85 to 0.93. Stepwise linear regression revealed that meat type did not contribute significantly to the regression model and generated a single linear regression equation for z-value calculations and D-value predictions for Korea/03 in both meat types. The z-value and the upper limit of the 95% confidence interval for the z-value were 4.64 and 5.32°C, respectively. From the lowest temperature to the highest, the predicted D-values and the upper limits of their 95% prediction intervals (conservative D-values) for 57 to 61°C were 241.2 and 321.1 s, 146.8 and 195.4 s, 89.3 and 118.9 s, 54.4 and 72.4 s, and 33.1 and 44.0 s. D-values and conservative D-values predicted for higher temperatures were 0.28 and 0.50 s for 70°C and 0.041 and 0.073 s for 73.9°C. Calculations with the conservative D-values predicted that cooking chicken meat according to current U.S. Department of Agriculture Food Safety and Inspection Service time-temperature guidelines will inactivate Korea/03 in a heavily contaminated meat sample, such as those tested in this study, with a large margin of safety.

Mechanism of secretion of plasma insulin-like growth factor-I into milk of lactating goats

1991 ◽  
Vol 131 (3) ◽  
pp. 459-466 ◽  
Author(s):  
C. G. Prosser ◽  
I. R. Fleet ◽  
A. J. Davis ◽  
R. B. Heap
Keyword(s):  
Growth Factor ◽  
Time Course ◽  
Specific Activity ◽  
Gel Filtration ◽  
Free Form ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Lactating Goats ◽  
Igf I ◽  
Growth Factor I

ABSTRACT 125I-Labelled insulin-like growth factor-I (IGF-I) was infused as the free form directly into the pudic artery supplying one gland of lactating goats (n = 6). The infusion was for 60 min and 0·4±0·09% (s.e.m.) of the infusate was secreted into milk from the infused gland during its first passage through that gland. A large proportion of the 125I-labelled IGF-I escaped into the systematic circulation and was secreted into milk of both glands. A total of 5·2±0·4% of infused radioactivity was recovered in milk from both glands from 0 to 720 min. Radioactivity consisted of trichloroacetic acid (TCA)-precipitable and -soluble counts which were shown by gel filtration to be authentic IGF-I and degraded products of the peptide. The amount and time course of TCA-soluble radioactivity in milk from both glands was similar, suggesting degradation of 125I-labelled IGF-I at extramammary sites. Maximum specific activity for 125I-labelled IGF-I in milk from the infused gland was reached 80–120 min after the start of infusion and was 2·5-fold greater than milk from the non-infused gland. The time course of appearance of 125I-labelled IGF-I in milk suggests that transfer was via the transcellular pathway and this was further supported by comparing the pattern of transfer of [14C]sucrose and [14C]amino acids. When excess unlabelled IGF-I was included in the infusate, specific activity in milk from the infused gland was reduced to that of the non-infused gland, indicating a competitive and saturable mechanism of secretion for 125I-labelled IGF-I. Comparison of uptake and secretion of 125I-labelled IGF-I into milk from the non-infused gland with that of endogenous immunoreactive IGF-I suggests that vectorial transport of IGF-I across the mammary gland may be a significant contributor of IGF-I levels in milk. Journal of Endocrinology (1991) 131, 459–466

scholarly journals Analysis of the forms of acetylcholinesterase from adult mouse brain

1975 ◽  
Vol 147 (2) ◽  
pp. 205-214 ◽  
Author(s):  
E D Adamson ◽  
S E Ayers ◽  
Z A Deussen ◽  
C F Graham
Keyword(s):  
Enzyme Activity ◽  
Mouse Brain ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Acetylcholinesterase Activity ◽  
Total Activity ◽  
Polyacrylamide Gel ◽  
Soluble Extract ◽  
Molecular Sizes

The solubilization of 80% of the acetylcholinesterase activity of mouse brain was performed by repeated 2h incubations of homogenates at 37 degrees C in an aqueous medium. Analysis of the soluble extract by gel filtration on Sephadex G-200 showed that up to 80% of the enzyme activity was eluted in a peak which was estimated to consist of molecules of about 74000mol.wt. This peak was called the monomer form of the enzyme. After 3 days at 4 degrees C, the soluble extract was re-analysed and was eluted from the column in four peaks of about 74000, 155000, 360000 and 720000 mol.wt. Since the total activity of the enzyme in these peaks was the same as that in the predominantly monomer elution profile of fresh enzyme, we concluded that the monomer had aggregated, possibly into dimers, tetramers and octomers. Extracts of the enzyme were analysed by polyacrylamide-gel electrophoresis and the resulting multiple bands of enzyme activity on gels were shown to separate according to their molecular sizes, that is by molecular sieving. All these forms had similar susceptibilities to the inhibitors eserine, tetra-isopropyl pyrophosphoramide and compound BW 284c51 [1,5-bis-(4-allyldimethylammoniumphenyl)pentan-3-one dibromide]. Thus the forms of the enzyme in mouse brain which can be detected by gel filtration and polyacrylamide-gel electrophoresis may all be related to a single low-molecular-weight form which aggregates during storage. This supports similar suggestions made for the enzyme in other locations.

scholarly journals Characterization of glycopeptides labelled from d-[2-3H]mannose and l-[6-3H]fucose in intestinal epithelial cell membranes during differentiation

1980 ◽  
Vol 192 (1) ◽  
pp. 145-153 ◽  
Author(s):  
A Herscovics ◽  
B Bugge ◽  
A Quaroni ◽  
K Kirsch
Keyword(s):  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Time Course ◽  
Cell Membranes ◽  
Alkali Treatment ◽  
Gel Filtration ◽  
Intestinal Epithelial ◽  
Membrane Glycoproteins ◽  
High Mannose ◽  
Fraction I

The labelled glycopeptides obtained by Pronase digestion of rat intestinal epithelial cell membranes were examined by gel filtration after injection of D-[2-3H]mannose and L-[6-3H]fucose. Three labelled fraction were eluted in the following order from Bio-Gel P-6, Fraction I, which was excluded from the gel, was labelled mostly with [3H]fucose and slightly with [3H]mannose. Fraction II contained “complex” asparagine-linked oligosaccharides since it was labelled with [3H]mannose and [3H]fucose, was stable to mild alkali treatment, and resistant to endo-beta-N-acetyl-glucosaminidase H. Fraction III contained “high-mannose” asparagine-linked oligosaccharides, which were labelled with [3H]mannose, but not with [3H]fucose; these were sensitive to endo-beta-N-acetylglucosaminidase H, and were adsorbed on concanavalin A-Sepharose and subsequently eluted with methyl alpha-D-mannopyranoside. The time course of incorporation of [3H]mannose into these glycopeptides in microsomal fractions showed that high-mannose oligosaccharides were precursors of complex oligosaccharides. The rate of this processing was faster in rapidly dividing crypt cells than in differentiated villus cells. The ratio of radioactively labelled complex oligosaccharides to high-mannose oligosaccharides, 3h after [3H]mannose injection, was greater in crypt than in villus-cell lateral membranes. Luminal membranes of both crypt and villus cells were greatly enriched in labelled complex oligosaccharides compared with the labelling in lateral-basal membranes. These studies show that intestinal epithelial cells are polarized with respect to the structure of the asparagine-linked oligosaccharides on their membrane glycoproteins. During differentiation of these cells quantitative differences in labelled membrane glycopeptides, But no major qualitative change, were observed.

scholarly journals Nutritional Properties and Oxidative Indices of Broiler Breast Meat Affected by Wooden Breast Abnormality

Animals ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 2272
Author(s):  
Krittaporn V. Thanatsang ◽  
Yuwares Malila ◽  
Sopacha Arayamethakorn ◽  
Yanee Srimarut ◽  
Nantawat Tatiyaborworntham ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Hypoxia Inducible Factor ◽  
Chicken Meat ◽  
Pyruvate Dehydrogenase Kinase ◽  
Breast Meat ◽  
Isoleucine Leucine ◽  
Lower Shear ◽  
Breast Abnormality ◽  
Pyruvate Dehydrogenase Kinase 1 ◽  
Wooden Breast

Wooden breast (WB) abnormality adversely impacts the quality of chicken meat and has been linked with oxidative stress. In this study, breast samples were taken from carcasses of 7-week-old Ross 308 broilers 20-min and 24-h postmortem. Five WB and seven non-WB control samples were assigned based on palpatory hardness (non-WB = no unusual characteristics and WB = focal or diffused hardness). WB exhibited lower contents of protein and the amino acids, i.e., isoleucine, leucine and valine, lighter surface color, lower shear force, greater drip loss and altered mineral profiles (p ≤ 0.05). Despite no difference in lipid oxidation, a greater degree of protein oxidation was found in the WB meat (p ≤ 0.05). Absolute transcript abundances of superoxide dismutase, hypoxia inducible factor 1 alpha and pyruvate dehydrogenase kinase 1 were greater in WB (p ≤ 0.05), whereas lactate dehydrogenase A expression was lower in WB (p ≤ 0.05). The findings support an association between oxidative stress and the altered nutritional and technological properties of chicken meat in WB.

Studies on the purification of Entamoeba histolytica antigens by gel filtration. II. The antigenic properties of the isolated fractions

1970 ◽  
Vol 16 (6) ◽  
pp. 493-498 ◽  
Author(s):  
Z. Ali Khan ◽  
E. Meerovitch
Keyword(s):  
Entamoeba Histolytica ◽  
Gel Filtration ◽  
Water Soluble ◽  
The Other ◽  
Soluble Extract ◽  
Serological Tests ◽  
Molecular Weights ◽  
Antigenic Properties ◽  
Water Soluble Extract

Partially purified fractions of the water-soluble extract of Entamoeba histolytica (DKB strain) obtained by chromatography in Sephadex G-200 (F1, F2, and F4) and G-100 (F3a, F3b, F3c, and F3d) gels were used in various serological tests and their reactivities compared with the whole 1:40 antigen. The main haemagglutinating (HA) and complement-fixing (CF) activities were confined to fractions F1 and F2, which had molecular weights of 650 000 and 229 000, respectively. The 4 to 6 μg/ml of protein contained in these fractions at the optimum dilution gave antibody liters comparable to those for the whole antigen, which had about 77 μg/ml of protein. The other antigen fractions (F4, F3a, F3b, F3c, and F3d) showed very little activity. Fraction F1 had two main precipitin bands (1 and 2), which showed reaction of identity with two of the bands in fraction F2. The other fractions which showed some HA and CF reactivity had trace amounts of these antigens. It is presumed that the antigens specific for precipitin bands 1 and 2 are the main CF and HA antigens.

OBSERVATIONS ON PROTEIN DIGESTION IN VIVO: II. DIETARY FACTORS AFFECTING THE RATE OF DISAPPEARANCE OF CASEIN FROM THE GASTROINTESTINAL TRACT

1959 ◽  
Vol 37 (12) ◽  
pp. 1475-1491 ◽  
Author(s):  
Carl Peraino ◽  
Quinton R. Rogers ◽  
Minoru Yoshida ◽  
Mou-Liang Chen ◽  
Alfred E. Harper
Keyword(s):  
Gastrointestinal Tract ◽  
Food Intake ◽  
Dietary Factors ◽  
Protein Digestion ◽  
Dietary Carbohydrate ◽  
Factors Affecting ◽  
Single Meal ◽  
Protein Free Diet ◽  
Stomach Emptying

The effects of various dietary changes on the emptying of solids and nitrogen from the stomach and on the disappearance of nitrogen from the gastrointestinal tract of rats trained to consume a single meal daily are described. When the animals were fed 5 g of food the presence of casein in the diet caused a general deceleration of stomach-emptying and altered the shape of the stomach-emptying curve. The presence of 50% of casein in the diet did not result in an accumulation of nitrogen in the intestine much above the amount found when a protein-free diet was fed. When dextrin was the dietary carbohydrate the diet emptied from the stomach as a homogeneous mixture, whereas when sucrose was the dietary carbohydrate the casein emptied from the stomach more slowly than did the other components of the diet. Raising the dietary level of fat to 50% caused a general deceleration of emptying and abolished the above-mentioned carbohydrate effect. No delay in stomach-emptying due to the presence of casein in the diet was noted when only 1.5 g of diet was fed. As the level of food intake was raised the total quantity of nitrogen emptying from the stomach per unit time increased although a greater percentage of the amount ingested emptied from the stomach when the level of food intake was low.

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