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M Pack

Publications and source records attributed to M Pack.

35 records · Page 2Linked to original sources
PubMed1996

Responses of growing and finishing turkey toms to dietary lysine.

The present study investigates the lysine requirements of British United Turkey (BUT) Big 6 turkey toms from 8 to 12 and from 16 to 20 wk of age. Growth, feed conversion, and carcass quality responses to increasing dietary lysine levels were measured. From 8 to 12 wk of age (4.0 to 8.8 kg live weight), about 1.20% (4.0 g/Mcal ME) lysine in the diet was found to be adequate to obtain optimum growth and feed conversion, Nitrogen retention also tended to increase with elevated dietary lysine levels in growing turkey toms. From 16 to 20 wk of age (13.1 to 18.5 kg live weight), the highest lysine level of 0.96% (3.0 g/Mcal ME) appeared to be insufficient to maximize weight gain. It is concluded, therefore, that the dietary lysine requirement of finishing turkey toms is 0.96% lysine or higher. In addition to the growth response, a marked increase in breast meat deposition in response to dietary lysine could be observed in finishing turkeys. Increasing dietary lysine decreased intramuscular fat content and grill loss and increased the protein level in breast meat.

Age Factors↗
PubMed1995

Effects of dietary sulphur-containing amino acids on performance and breast meat deposition of broiler chicks during the growing and finishing phases.

1. Two growth trials were performed to measure the effects of dietary methionine and cystine (SAA) on growth rate, food conversion efficiency and breast meat deposition in male broilers. 2. In experiment 1, broilers were grown on 6 experimental diets covering a range from 6.9 to 9.6 g SAA/kg. The diets were fed from 15 to 33 d of age. Similarly, in experiment 2, 6 diets containing 6.0 to 8.5 g SAA/kg were fed to finishing broilers 33 to 43 d of age. In each experiment 60 birds per treatment were processed, and carcase yield and breast meat percentage were determined. 3. Significant responses in weight gain, efficiency of food conversion and breast meat percentage were detected, which could be described well by exponential regression curves. Dietary SAA requirements to obtain maximum efficiency of food utilisation and maximum breast meat deposition were estimated to be about 9.0 g/kg from 15 to 33 d of age, and about 8.0 g/kg from 33 to 43 d of age. 4. Economic aspects were considered to calculate optimum SAA specifications from the results. In both trials, the dietary optimum of SAA was found to be higher for birds to be further processed than for birds to be marketed as whole carcases.

Animals↗
PubMed1995

Effects of dietary sulfur amino acids and crude protein on the performance of finishing broilers.

The effects of different combinations of dietary methionine + cystine (Met + Cys) and dietary crude protein (CP) in finishing broilers were investigated in two growth studies. In Exp. 1, male broilers 29 to 42 days of age were fed 18 diets containing 16.9%, 18.7%, or 20.4% CP with six levels of Met + Cys within each protein level. Similarly, in Exp. 2 another 12 diets containing either 18.0 or 21.5% CP were fed to male broilers 29 to 48 days of age. In general, the Met + Cys requirement for optimum feed conversion was higher than for maximum growth. In both experiments, between 0.80% and 0.85% methionine + cystine optimized feed conversion. These dietary levels were valid for a 13.05 MJ ME/kg diet fed to broilers growing from 1.2 kg to 2.2 kg (Exp. 1), or for a 13.60 MJ ME/kg diet fed to broilers growing from 1.3 kg to 3.0 kg (Exp. 2). The Met + Cys requirement was not consistently affected by the dietary CP content in Exp. 1. In Exp. 2, increasing dietary CP from 18.0% to 21.5% tended to increase the Met + Cys requirement for optimum feed conversion. A dietary CP level of 18.0% to 18.7% supported performance and carcass fat deposition equal to diets containing 20.4% or 21.5% CP, respectively, when the sulfur amino acid content was adequate.

Aging↗
PubMed1995

Free amino acids can replace protein-bound amino acids in test diets for studies in rainbow trout (Oncorhynchus mykiss).

Effects of reducing dietary concentration of protein-bound amino acids on growth, feed intake and composition of gain in rainbow trout were studied in four experiments. Average initial body weights ranged between 29 +/- 0.7 and 55 +/- 0.5 g per trout. Diets contained approximately 20 MJ digestible energy/kg dry matter. Each diet was fed to satiation to four replicate groups of 20 trout. Feed intake and growth rates were recorded for each group. Body composition was analyzed in representative groups at the start of each experiment and in all experimental groups at the end of each experiment. Reduction of dietary protein concentration to < 380 g/kg dry matter caused significantly lower growth rates and reduced protein concentrations of gain, but these reductions in growth could be offset by the addition of 10 crystalline essential amino acids. Fish meal was completely replaced by a mixture of wheat gluten and crystalline amino acids without negative influences on growth. In the absence of fish meal, almost half the wheat gluten could be replaced by crystalline amino acids in diets containing about 32 g N x 6.25/kg dry matter without significant influences on growth. In such diets, concentrations of individual amino acids may be varied widely with no variation in other amino acids or nutrients.

Amino Acids↗
PubMed1995

Response of rainbow trout (Oncorhynchus mykiss) growing from 50 to 150 g to supplements of DL-methionine in a semipurified diet containing low or high levels of cystine.

We studied the effect of increasing dietary concentrations of DL-methionine on growth, feed intake, feed conversion ratio and the composition of gain in rainbow trout. Twenty-four groups of 20 trout initially weighing 51 +/- 0.5 g/trout were fed semipurified diets containing 20.1 MJ digestible energy and either 3.0 or 5.8 g cystine/kg dry matter. At each level of cystine, 12 levels of methionine (2 to 11 g/kg dry matter) were achieved by supplementation with graded quantities of DL-methionine. During an experiment of 49 feeding days, no significant effect of the level of dietary cystine was found for any performance trait. Nonlinear responses to increasing dietary methionine concentrations were found for feed intake, growth rate, protein concentration of gain and protein deposition, whereas fat concentration of gain decreased concurrently. Dietary methionine was utilized most efficiently at a concentration of 3.5 g methionine/kg dry matter or 0.17 g/MJ digestible energy. Ninety-five percent of the plateau deposition of body protein was achieved at a dietary methionine concentration of 8 g/kg dry matter or 0.40 g/MJ digestible energy. For achieving 98%, the required concentration was 9.0 g/kg or 0.49 g/MJ. Recommended dietary methionine concentration will depend on the trait chosen.

Animal Feed↗
PubMed1995

Response of rainbow trout (Oncorhynchus mykiss) growing from 50 to 170 g to supplements of either L-arginine or L-threonine in a semipurified diet.

We studied the effects of increasing dietary concentrations of either L-arginine or L-threonine on growth, feed intake, feed conversion ratio and composition of gain in rainbow trout. Semipurified diets containing 20.1 MJ digestible energy/kg dry matter, with wheat gluten and crystalline amino acids as sole sources of amino acids, were fed to rainbow trout (initial mean body weight 47 +/- 0.7 g). In one series of 12 diets, arginine concentration ranged from 5.0 to 23.8 g/kg dry matter; in a second series of 12 diets, threonine concentration ranged from 3.7 to 21.0 g/kg dry matter. Each diet was fed to a group of 20 fish. During the experiment of 51 feeding days, dry matter intake, weight gain, feed conversion ratio, protein concentration of gain and total protein deposition followed exponential functions. For achieving 95% of the potential maximum protein deposition, dietary concentrations of 11.6 g arginine and 10.4 g threonine/kg dry matter were required. Arginine and threonine were both utilized most efficiently at dietary concentrations of approximately 6 g/kg dry matter. At low dietary concentrations of arginine, deposition of this amino acid exceeded the quantity fed. Recommended dietary concentrations of arginine and threonine will depend on the trait desired in the trout.

Animal Feed↗
PubMed1995

Sulfur amino acid requirement of broiler chicks from fourteen to thirty-eight days of age. 1. Performance and carcass yield.

Two experiments were conducted to evaluate increasing dietary levels of methionine and TSAA on broiler performance and carcass yield. In Experiment 1, the corn-soybean basal diet contained .75% TSAA, to which increasing dose levels of DL-methionine were added, providing at the highest supplemental level .95% TSAA. The experimental diets were fed for 20 d, covering the age period of 14 to 34 d. In Experiment 2, a corn-soybean basal diet containing .70% TSAA was used along with DL-methionine supplements to determine TSAA requirement during the age period of 14 to 38 d. The highest supplemental level of DL-methionine in this experiment provided .94% TSAA. The TSAA requirement was found to be higher for maximum efficiency of feed utilization and breast meat yield than for obtaining maximum weight gain. Based on feed conversion efficiency and breast meat yield, the requirement for TSAA was estimated to be at least .88% for the age period of 14 to 34 or 38 d. It was calculated that the estimated TSAA requirement was equivalent to approximately .75% apparent digestible SAA or .78% true digestible SAA.

Age Factors↗
PubMed1995

Sulfur amino acid requirement of broiler chicks from fourteen to thirty-eight days of age. 2. Economic evaluation.

A calculation model was developed that can be used to derive dietary methionine and cystine (TSAA) levels for maximum profitability in growing broilers. Based on dose-response curves from two broiler experiments, the model calculates additional income from improved feed conversion and from increased breast meat yield. From the comparison of additional income to the additional cost associated with increasing dietary TSAA levels, the TSAA content giving maximum profit can be estimated. Under European price conditions, a dietary level of .95% TSAA was found to be most profitable for broilers grown to 1.7 kg (Experiment 1, 14 to 34 d of age), when only the feed conversion response to dietary TSAA was considered. In broilers grown to 2.2 kg (Experiment 2, 14 to 38 d of age), two situations were simulated. If only the feed conversion response was evaluated, the most profitable TSAA level would be .85%. If both feed conversion and breast meat responses were considered, a higher level of .89% TSAA would be optimum. Changing prices of input and output variables (broiler feed, breast meat, DL-methionine) affected the respective economic optimum level of dietary TSAA only slightly.

Age Factors↗
PubMed1994

Biological efficacy of L-lysine preparations containing biomass compared to L-lysine-HCl.

In two growth experiments on broilers of 6 to 27 days of age, the biological efficacy of three L-lysine preparations containing biomass was evaluated in comparison to L-lysine.HCl. L-lysine from the different sources was added in graded levels to a basal diet deficient in lysine, but adequate in all other nutrients. From multi-exponential regression analysis of weight gain and feed conversion responses, biological efficacy of the three L-lysine preparations containing biomass was estimated to be 97%, 103%, and 113%, respectively. None of these estimates was significantly different from 100%. Thus, it is concluded that the efficacy of the L-lysine preparations to deliver lysine is equivalent to L-lysine.HCl.

Animal Feed↗
PubMed1991

Completion of the last half of the structure of the human gene for the Pro alpha 1 (I) chain of type I procollagen (COL1A1).

The nucleotide sequences of the 3'-half of the human gene for the pro alpha(I) chain of type I procollagen (COL1A1) is presented. The results provide the nucleotide sequences for 26 introns not previously analyzed. The sequences that are presented, together with those previously published, make it possible to design primers for the polymerase chain reaction for amplifying and sequencing the gene. The availability of such primers will greatly facilitate the current search for mutations that can cause common and rare diseases of connective tissue.

Base Sequence↗
PubMed1990

Phenotypic heterogeneity in osteogenesis imperfecta: the mildly affected mother of a proband with a lethal variant has the same mutation substituting cysteine for alpha 1-glycine 904 in a type I procollagen gene (COL1A1).

A proband with a lethal variant of osteogenesis imperfecta (OI) has been shown to have, in one allele in a gene for type I procollagen (COL1A1), a single base mutation that converted the codon for alpha 1-glycine 904 to a codon for cysteine. The mutation caused the synthesis of type I procollagen that was posttranslationally overmodified, secreted at a decreased rate, and had a decreased thermal stability. The results here demonstrate that the proband's mother had the same single base mutation as the proband. The mother had no fractures and no signs of OI except for short stature, slightly blue sclerae, and mild frontal bossing. As a child, however, she had the triangular facies frequently seen in many patients with OI. On repeated subculturing, the proband's fibroblasts grew more slowly than the mother's, but they continued to synthesize large amounts of the mutated procollagen in passages 7-14. In contrast, the mother's fibroblasts synthesized decreasing amounts of the mutated procollagen after passage 11. Also, the relative amount of the mutated allele in the mother's fibroblasts decreased with passage number. In addition, the ratio of the mutated allele to the normal allele in leukocyte DNA from the mother was half the value in fibroblast DNA from the proband. The simplest interpretation of the data is that the mother was mildly affected because she was a mosaic for the mutation that produced a lethal phenotype in one of her three children.

Alleles↗
PubMed1989

Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific.

Recent reports have demonstrated that a series of probands with severe osteogenesis imperfecta had single base mutations in one of the two structural genes for type I procollagen that substituted amino acids with bulkier side chains for glycine residues and decreased the melting temperature of the triple helix. Here we demonstrate that the type I procollagen synthesized by cultured fibroblasts from a proband with a severe form of osteogenesis imperfecta consisted of normal molecules and molecules over-modified by post-translational reactions. The thermal stability of the intact type I collagen was normal as assayed by protease digestion under conditions in which a decrease in thermal stability was previously observed with eight other substitutions for glycine in the alpha 1(I) chain. In contrast, the thermal stability of the one-quarter length B fragment generated by digestion with vertebrate collagenase was decreased by 2-3 degrees C under the same conditions. Nucleotide sequencing of cDNAs and genomic DNA established that the proband had a substitution of A for G in one allele of the pro alpha 1(I) gene that converted the codon for alpha 1-glycine 844 to a codon for serine. The results also established that the alpha 1-serine 844 was the only mutation that could account for the decrease in thermal stability of the collagenase B fragment. There are at least two possible explanations for the failure of the alpha 1-serine 844 substitution to decrease the thermal stability of the collagen molecule whereas eight similar mutations decreased the melting temperature. One possibility is that the effects of glycine substitutions are position specific because not all glycine residues make equivalent contributions to cooperative blocks of the triple helix that unfold in the predenaturation range of temperatures. A second possible explanation is that substitutions of glycine by serine have much less effect on the stability of protein than the substitutions by arginine, cysteine, and aspartate previously studied.

Cell Line↗
PubMed1983

Interferon-induced differentiation of U937 cells. Comparison with other agents that promote differentiation of human myeloid or monocytelike cell lines.

Effects of human fibroblast (beta) or leukocyte (alpha) interferon (IFN) on differentiations of a human histiocytic lymphoma-derived cell line (U937) or promyelocytic leukemia-derived cell line (HL-60) were studied. When cultured with beta-IFN (400-1,000 U/ml), U937 cells showed gross morphologic and microscopic changes consisting of clumping, increased cytoplasmic-to-nuclear ratio, enhanced prominence of cytoplasmic granules, and membrane ruffling. After culture with beta-IFN, the number of U937 cells reactive with B43.4.1 monoclonal antibody, which is specific for human monocytes, natural killer cells, and neutrophils, increased from less than 10% of U937 cells to 47% beta-IFN treatment also enhanced antibody-dependent cellular cytotoxicity against chicken erythrocytes by U937 cells. The same morphologic, phenotypic, and functional changes were also observed when U937 were treated with recombinant or natural alpha-IFN. The effects of alpha-IFN were totally abolished by anti-alpha-IFN serum. In contrast, HL-60, which differentiates toward cells of the monocyte lineage in response to phorbol 12-myristate 13-acetate (based on the above criteria), and toward granulocytes in response to dimethyl sulfoxide, did not differentiate when cultured with alpha- or beta-IFN. No consistent relationship between induction of differentiation and changes in phospholipid methylation were observed.

Antigens↗
PubMedDate not supplied

The wheel of care.

Explore the source record for details and available documents.

Communication↗
PubMedDate not supplied

Integration of periorbital titanium implants in irradiated bone: case report and histologic evaluation.

Extraoral implants are used increasingly frequently in the wake of ablative tumor surgery and adjuvant radiation or chemotherapy for craniofacial rehabilitation with facial prostheses and epitheses. However, high rates of nonintegration and implant loss have been reported for extraoral implants, especially for those in the periorbital region following irradiation. This case report and corresponding histologic evaluation describe the osseointegration pattern in irradiated periorbital bone, based on the example of 3 retrieved, clinically integrated, stable titanium screw implants.

Adult↗