Barbara Dolińska

Effect of iodine-enriched yeast supplementation of diet on performance of laying hens, egg traits, and egg iodine content

The aim of the study was to evaluate the effect of iodine yeast (I-yeast) supplementation on the performance, egg traits, and iodine content of eggs of laying hens. The experiment was conducted as a completely randomized design. A total of 60 laying hens (Hy-Line Brown), 25 wk of age, was divided into 3 groups (4 replicates), and a feeding experiment was conducted for 12 wk. The concentrations and forms of iodine added to the basal diet were as follows: control group, 1 mg of iodine/kg of feed, Ca(IO(3))(2)•H(2)O; experimental groups E1 and E2, 1 and 2 mg of iodine per kilogram of feed, I-yeast, respectively. The iodine yeast did not significantly affect BW gain. Lower level of hen day egg production for groups E1 and E2 was not confirmed statistically; however, it was probably the consequence of low replication. Feed intake was the lowest in the E1 group and feed conversion rate was the highest in the E2 group. Furthermore, the egg and albumen weight was the highest in the group supplemented with 2 mg/kg of iodine from I-yeast (P < 0.05). The concentration of iodine in the egg yolk from groups E1 and E2 was respectively about 80 and 90% higher, compared with the control group. Eggshells from the group fed with 2 mg/kg of I-yeast contained almost 3 times more iodine than eggshells from the control group. The results suggest that iodine yeast supplementation in the diet of laying hens is an effective method for increasing iodine concentration in eggs and thus could contribute to elimination of iodine deficiency disorders in humans consuming iodine-enriched eggs.

Comparing the effect of Biolasol® and HTK solutions on maintaining proper homeostasis, indicating the kidney storage efficiency prior to transplantation.

BACKGROUND Maintaining proper homeostasis involving normal physiological level of extra- and intracellular solutions is one of the factors that determine restoring the life functions of a transplanted organ. The aim of this study was to demonstrate the effectiveness of the newly developed Biolasol(®) solution in kidney storage and to compare its protective effect to the standard HTK solution. MATERIAL/METHODS Isolated porcine kidneys were perfused, preserved (24 and 48 h) and reperfused with Biolasol(®) and HTK solutions. The perfusate samples were used to analyze pH; the amount of released indicator enzymes aspartate aminotransferase (AST), alanine aminotransferase (ALT), and lactate dehydrogenase (LDH); and the concentration of sodium, potassium and magnesium. RESULTS Kidney storage in the HTK liquid may cause metabolic acidosis after 24 and 48 hour preservation (pH drop below 6.8). pH of perfusates sampled after perfusion and reperfusion with Biolasol(®) solution was within the range 6.8-7.7. The content of sodium ions during perfusion and reperfusion was the closest to the reference values while using the Biolasol(®) solution. Only Biolasol(®) ensured normal homeostasis of Mg2+ ions. In the presence of the HTK solution their level was significantly (more than 1000%) higher than the normal physiological value. For both solutions, ALT and AST activities were within the normal range or differed only slightly. CONCLUSIONS Biolasol(®) and HTK solutions protect kidneys against ischemic damage. Still, Biolasol(®) offers better homeostasis maintenance, which may suggest it more effectively preserves kidneys prior to transplantation.

The properties of solid Zn(II)–amino acid complexes in the form of suspensions

An investigation was made into the experimental conditions for the formation of poorly soluble complexes of the divalent Zinc(II) combined with the following selected amino acids: tyrosine, tryptophan, cysteine, histidine, and alanine, in the form of suspensions for parenteral administration. The number of Zn(II)-binding sites in the amino acid (n) as well as the amino acid affinity to Zn(II) (Ka), were determined. Cysteine was found to have the highest number of Zn(II)-binding sites--3, whereas alanine the lowest--1. In the conditions described herein, Zn(II) amino acid complexes of diverse stability (durability) were obtained. The analysis of the kinetics of the binding revealed that the most stable complexes were those formed by Zn(II) in combination with tryptophan (Ka = 405.78 microM(-1) +/- 12.17), and with tyrosine (Ka = 343.88 microM +/- 22.35); whereas the least stable complexes were those formed by Zn(II) in combination with histidine (Ka = 29.90 microM +/- 4.78), and with alanine (Ka = 13.0 microM(-1) +/- 1.04). Cysteine formed complexes of intermediate stability (Ka = 168.53 microM(-1) +/- 12.36). The stability ofthe Zn(II) amino acid complexes obtained was conditioned by both the molecular weight (P = 0.033) of the amino acid and its isoelectric point (P < 0.001).

The effect of selected antioxidants on the kinetics of changes in the stability of an HTK solution: a technical note.

Summary and ConclusionsThe effect of selected antioxidants (vitamin C, cysteine, fumaric acid) on the stability of a 0.3-mM solution of HTK has been determined. The stability of the HTK solution was determined using the changes in histidine content at elevated temperatures. The rate of the amino acid decomposition in this solution was 42.3% lower than in a solution without an antioxidant.Vitamin C is the most effective antioxidant. An HTK solution stored at +5°C is stable for 450 days with vitamin C added to it, for 265 days with cysteine, for 242 days with fumaric acid, and for 260 days with no antioxidant.

The Effect of HTK Solution Modification by Addition of Prolactin on Biochemical Indices Reflecting Ischaemic Damage to Porcine Kidney

INTRODUCTION The aim of our study was to evaluate the impact of perfusion with HTK solution, modified by the addition of prolactin (PRI), on selected biochemical parameters of porcine renal damage within 24 and 48 hours after the onset of cold ischemia time. METHODS Each study group consisted of 10 adult pigs. During harvesting the kidneys were rinsed with Ringers solution (group 1), HTK (group 2), and HTK+PRL in a dose of 0.2 mg/dL, 0.02 mg/dL, and 0.01 mg/dL in groups 3, 4 and 5, respectively. The levels of lactate dehydrogenase, asparagine (AST) and alanine aminotransferases, lactates, total protein, potassium and calcium were determined in the perfusate. After 24 and 48 hours the rinsing procedure and the abovementioned tests were repeated. RESULTS After 24 hours of storage, in 4 groups, significantly lower levels of LDH (U/L) were recorded compared with HTK solution alone, namely 235 ± 93 versus 271 ± 125 (perfusion minute, 0), and 55 ± 21 versus 125 ± 94 (30th minute). Similar behavior pattern was presented by AST (U/L) and potassium (mmol/L), and the results were 31 ± 8 versus 35 ± 12 and 16 ± 10 versus 29 ± 14, and 12 ± 3 versus 16 ± 3 and 10 ± 1 versus 13 ± 1, respectively. The changes described above were not observed in the 48th hour of reperfusion. CONCLUSION Our study results indicate the possibility of cytoprotective action of PRL after adding it to the fluid perfusing kidneys during cold ischemia. This effect, observed after 24 hours of storage, was to a considerable extent dose dependent. In our experiment the effect was pronounced only at 0.02 mg/dL supply of PRL.

Sustained release and biological availability of dalarelin from the biodegradable coacervate microcapsules.

A complex coacervation method was used to prepare microcapsules containing 74.8 +/- 1.5% of the 125I labelled dalarelin incorporated in the gelatine-algin coating. Microcapsules (62 +/- 1.7%) formed, did not exceed a size of 108 microm. The high content of the small size allowed this formulation to be administered by intramuscular injection to rats. It was found that the 125I labelled dalarelin in the form of microcapsules had better bioavailability and was active longer in the rat when compared with the 125I labelled dalarelin solution injections. Dalarelin administered in the microcapsular form was characterised by a higher biological availability. The degree of relative biological availability was calculated as 123% for the dalarelin in the microcapsular form.

Hepatoprotective Effect of Prolactin and Cysteine Contained in Perfusion and Preservation Solutions on Porcine Liver Stored in Simple Hypothermia

INTRODUCTION The aim of our study was to determine the results of histidine-tryptophan-ketoglutarate (HTK) solutions modified by the addition of the antioxidant cysteine (Cys), and of prolactin (PRL) on storage of isolated porcine livers. METHODS We measured in the media of isolated livers stored for 24 hours in HTK (control group) or modified HTK+Cys (0.3 mmol/L)+PRL (3 IU/L study group) the amounts of aspartate aminotransferase (AST), alanine aminotransferase (ALT), lactate dehydrogenase (LDH), lactic acid as well as Ca (II), Mg (II), Na (I) and K (I) ions during a 30-minute perfusion after 24 hours of storage. RESULTS All tested markers were released more slowly into HTK+Cys+PRL with less release of K(I) and Mg(II) and greater of Na(I) and Ca(II) ions. CONCLUSIONS Addition of the Cys and PRL to HTK positively affected 24-hour storage of isolated livers.

The Influence of Condition on Permeation of Ca(II) Ions from Solutions of Selected Calcium’s Salts Through Model Membrane

The permeation of calcium’s ions from calcium solutions of fumarate, gluconate, and citrate through model membrane from the donor chamber to the acceptor chamber has been examined. Process was traced depending on the concentration of the appropriate calcium’s salts (1, 2.5, and 5 mmol/l) and pH value of acceptor environment (1.3, 6.2, and 7.4) which imitated natural conditions appearing in the digestive tract. The amount of permeating Ca(II) ions (percent) and their Ca(II) availability AUC (0–6 h) has been determined. In dependence on the conditions, penetration was as follows: 30.3–95.2% of calcium ions from fumarate solution; 73.0–90.1% of Ca(II) from citrate solution; and 19.0–95.0% of Ca from gluconate solution. The investigation indicates that the amount of permeated Ca(II) ions and their availability are connected with the concentration of the calcium salt and pH of acceptor environment. Fumarate and citrate are available at pH value of acceptor environment 1.3 and 6.2 and gluconate at the pH value of 6.2 and 7.4. These substances are practically unavailable from the acceptor environment at pH value 1.3 for gluconate and 7.4 for fumarate. Results suggest that calcium citrate can be available for organism independently from pH value of acceptor environment.

Preparation and properties of selected Zn(II)-peptide complexes in suspension.

The preparation and properties of low soluble, suspended Zn(II) complexes containing the selected peptides: tyroliberin (TRH), gonadorelin (GnRH), dalarelin and corticothropin (ACTH) were studied. The amount of Zn(II) bound by 1 muM of the selected peptide (n) was defined, as well as affinity of Zn(II) to the peptide (Ka) and the durability of the created complex Zn(II)-peptide (Kd). ACTH associated the highest amount of Zn(II), and GnRH the lowest one: 1 microM of ACTH complexed 0.81 microM +/- 0.03 Zn(II), the same quantity of GnRH-0.52 microM +/- 0.07 and TRH and dalarelin associated 0.75+/-0.03 and 0.79+/-0.02 microM of Zn(II), respectively. The closest affinity was stated between Zn(II) and GnRH (Ka=157.692+/-21.300 microM(-1)), the smallest-towards ACTH (Ka=1.136+/-0.042 microM(-1)). The lower amount of Zn(II) associated by the studied peptide, the higher was its affinity versus this metal (r=-0.942). The analysis of the kinetics of the Zn(II)-peptide linkage revealed that the most stable complexes with this metal were formed by GnRH (Kd=0.006+/-0.001 microM(-1)) and by dalarelin (Kd=0.020+/-0.001 microM(-1)). Zn(II) with GnRH complexes are about 147 times more durable than ACTH (Kd=0.880+/-0.033 microM(-1)) ones. It was established that the Zn(II)-peptide complexes were more stable in the case of lower molecular weight of the peptide (r=0.963), and the inferior number of the amino acid residues accessible in the peptide (r=0.967).

The Effect of HTK Solution Modification by Addition of Thyrotropin and Corticotropin on Biochemical Indices Reflecting Ischemic Damage to Porcine Kidney

INTRODUCTION The aim of our study was to evaluate the impact of perfusion with HTK (histidine-tryptophan-ketoglutarate, Custodiol®, Dr. Franz Kohler Chemie, Germany) solution, modified by the addition of porcine thyroid-stimulating hormone (TSH) and corticotropin (ACTH), on selected biochemical parameters of porcine renal damage within 24 and 48 hours after the onset of cold ischemia time. METHODS Each study group consisted of 10 adult pigs. During harvesting the kidneys were rinsed with Ringer solution (group 1), HTK (group 2), HTK-TSH (1 μg/dL) or HTK-ACTH (1 μg/dL) in groups 3 and 4. The solutions were cooled to 4°C-6°C. Within 30 minutes of the first perfusion, the discharged fluid was clear and the kidneys cooled to 4°C. The levels of lactate dehydrogenase, asparagine and alanine aminotransferases, lactates, total protein, potassium, calcium, and pH were determined in the perfusate. After 24 and 48 hours the rinsing procedure and the above-mentioned tests were repeated. Differences between the means of 2 independent samples were tested with a nonparametric Mann-Whitney U test. RESULTS As the result of hormone addition, in both time intervals it was possible to observe considerably lower protein concentrations (g/L) in perfusates compared with HTK solution, without an addition. At 24 hours, we measured following values: 36 ± 4, 8 ± 3 and 6 ± 1 versus 48 hours, 34 ± 1, 2 ± 1, and 4 ± 1 in groups 2, 3, and 4. A similar pattern was observed with LDH (U/L) at 48 hours: 662 ± 89, 374 ± 151, and 386 ± 111, respectively. Lactate concentrations (mmol/L) were then significantly higher: 1.4 ± 0.3 in the TSH group and 1.2 ± 0.5 in the ACTH group as opposed to 0.2 ± 0.1 in unmodified HTK group. CONCLUSION We observed the possibility of cytoprotective actions of TSH and ACTH addition to the perfusion fluid during cold ischemia, positive effects that were especially visible upon prolonged 48-hour storage.