Action of egg lysozyme on representatives of the family Micrococcaceae. The action on staphylococci

The results of the study on the effect of various concentrations of lysozyme on staphylococci of three species, i.e. Staphylococcus aureus, Staphylococcus epidermidis and Staphylococcus saprophyticus are presented. The study was performed with the use of the turbidimetric method. It was found that all the staphylococci had a common tendency for changing the optic density (OD) of the suspensions under the effect of lysozyme which was different from that in Micrococcus luteus. However, the dynamics of decreasing the OD in Staph. saprophyticus was characterized by some properties which provided a supposition that the structures of the cell walls in Staph. aureus and Staph. epidermidis were close, while the cell walls in Staph. saprophyticus had some unknown characteristics.     

Effects of egg yolk testosterone on growth and immunity in a precocial bird

In oviparous vertebrates, maternal steroid allocation to eggs can have important fitness consequences for the offspring. However, elevated testosterone levels are not only associated with beneficial postnatal effects, such as enhanced growth and high social status, but may also entail costs by suppressing the immune system. In this study, testosterone levels in eggs of Chinese painted quail (Coturnix chinensis) were experimentally manipulated to evaluate its effects on growth and immunocompetence. Testosterone did not affect embryonic development, body size or growth during the first 20 days. However, elevated testosterone levels during embryonic development were immunosuppressive for chicks with inherently higher growth rate. Adaptive scenarios where only beneficial effects of increased testosterone levels are considered may therefore need to be re-evaluated.     

Occurrence of glycosphingolipids in chicken egg yolk.

Chicken egg yolk was found to contain a unique glycosphingolipid pattern not seen in other types of tissue or cell. These glycosphingolipids were isolated in pure form and their structures established by sequential enzymic hydrolysis and permethylation analysis. The major gangliosides in chicken egg yolk are N-acetylneuraminosylgalactosylceramide, N-acetylneuraminosyl-lactosylceramide and di-N-acetylneuraminosyl-lactosylceramide. The only neutral glycosphingolipid found in chicken egg yolk is galactosylceramide.     

31P-NMR characterization of hen egg yolk and egg white

The avian egg is an isolated system where embryonic development can easily be studied. Furthermore, the system can be subjected to various environmental constraints. Its size is such that it can easily be accommodated in most NMR instruments. This is demonstrated by a recent 31P-NMR surface coil experiment where the increase of embryo size and development could be judged by the levels of ATP and phosphocreatine (Belton, P.S., Gordon, R.E., Jones, J.M. and Shaw, D. (1983) Br. Poult. Sci. 24, 429-433).     

Thermotropic behavior of liposomes from egg yolk lecithin, hydrogenized egg yolk lecithin and their mixtures

The thermotropic properties of multilamellar liposomes from egg yolk lecithin, hydrogenized egg yolk lecithin and several mixtures of these two lipids were studied with the application of excimer--forming optical probe pyrene and microcalorimetry. It was discovered that when the proportion of the egg yolk lecithin in the lipid mixture was raised the temperature of the main phase transition reduced. For all this, independent of the lipid mixture composition when the temperature was raised, apparently, polarity of pyrene microenvironment in the liposomes bilayers decreased. On the basis of the analysis of solidus and liquidus curves obtained from calorimetric studies of the lipid mixtures and bend points of Arrhenius anamorphose obtained during the pyrene excimer formation measurements some conclusions were made about the role of unmodified and hydrogenized egg yolk lecithin cluster formation in the determination of thermotropic properties of the liposomes from the above two lipids mixtures. High temperature phase transition discovered for the egg yolk lecithin while measuring the pyrene excimer formation is proposed to be closely connected with temperature-dependent changes in the organization of phospholipid heads on the interphase bilayer/H2O solution.     

鸭蛋黄颜色的生态遗传分析

1 引言 蛋黄颜色作为衡量禽蛋质量的主要经济性状之一,愈来愈受到消费者的关注,家鸡中这种性状的遗传力很低。Farnsworth等(1955)发现其遗传力为0.15,Torges报道其仅为0.05,Vanchev等(1980)估测母系遗传力为0.18,父系为0.47。因此,决定蛋黄色度主要是饲料因素,饲料中的氧化类胡萝卜素(叶黄素和玉米黄质)为蛋黄提供色素来源,能大量提供有效类胡萝卜素的饲料有藻类、紫花苜蓿、黄(白)玉米、大豆等植物,甲壳类动物、微生物(醇母)及类胡萝卜素制剂Mackey分别用墨角藻(Fucus vesiculosus)、齿缘墨角藻     

Effects of egg yolk and glycerol levels in lactose-EDTA-egg yolk extender and of freezing rate on the motility of frozen-thawed stallion spermatozoa

Two experiments were designed to evaluate the effects of egg yolk and glycerol concentrations, freezing rate, and clarification of a lactose-EDTA-egg yolk extender on the post-thaw motility of stallion spermatozoa. In both experiments there was no influence of freezing rate (vapor vs controlled) on the percentage of progressively motile spermatozoa after thawing. Furthermore, no significant interaction among treatments was detected. In Experiment 1, clarified (centrifuged at 34,400 × g for 30 min) lactose-EDTA-egg yolk extenders containing 16 or 20% egg yolk and 3 or 4% glycerol were superior to those containing 12% egg yolk or 2% glycerol, based on the percentage of progressively motile stallion spermatozoa at 0, 30, 60, and 90 min after thawing. However, in Experiment 2, clarification of the lactose-EDTA-egg yolk extender was detrimental to the ability of the stallion spermatozoa to survive after thawing; 4% glycerol was superior to 2% glycerol. The best extender based on the percentage of progressively motile spermatozoa after thawing was nonclarified lactose-EDTA-egg yolk extender containing 20% egg yolk and 4% glycerol.     

Effects of egg yolk proteins on the longitudinal bone growth of adolescent male rats

Hen egg is a nutritional store for a new life. We examined the effect of egg yolk proteins on longitudinal bone growth in the rat. Protein fractions from egg yolk were tested. Milk protein, casein, was used as a control. The bone growth rate was significantly increased by yolk water-soluble protein (YSP, 100 mg/kg) administration for 5 d. The bone morphogenetic protein-2 immunostaining of growth plate was also increased. Considering the results, YSP can be used as a growth-promoting factor.     

Apolipoproteins and lipoprotein families in chicken embryos and egg yolk.

1. Turkey anti-LP-A and anti-LP-B cross react strongly with whole adult chicken serum. 2. Similar reactions occur with whole chicken embryo sera (10-21 days of incubation) and egg yolk fluid. 3. Ultracentrifugation of sera from 14-day old chicken embryos, after reaction with anti-LP-B, reveal complete precipitation of the VLDL and LDL of embryo serum (indicating that adult-type LP-B is the major apolipoprotein of these density classes). 4. All of the chicken embryo adult-type apo-LP-A is in the HDL fraction. 5. However, egg yolk and hen serum VLDL contain apo-LP-A as well as apo-LP-B.     

Nature of the thiamin-binding protein from chicken egg yolk.

A simple, rapid and efficient procedure for the purification of thiamin-binding protein from chicken egg yolk was developed. The method involved removal, by exclusion, of lipoproteins from DEAE-cellulose and subsequent elution of water-soluble proteins held on the ion-exchanger with 1 M-NaCl, followed by treatment of the eluted protein fraction with an aqueous suspension of dextran/charcoal to generate apoprotein from the holoprotein. The resultant protein fraction was subjected to bioaffinity chromatography on thiamin pyrophosphate--AE (aminoethyl)-Sepharose. The protein eluted specifically with 10 microM-thiamin at pH 7.0, was homogeneous by the criteria of polyacrylamide-gel disc electrophoresis, had a mol.wt. of 38 000 +/- 2000 and was not a glycoprotein. The purified thiamin-binding protein specifically interacted with riboflavin-binding protein with no detectable deleterious affect on its (14C)thiamin-binding capacity. The protein bound [14C]thiamin with a molar ratio of 1.0, with dissociation constant (Kd) 0.41 microM. This protein-ligand interaction was inhibited by thiamin analogues and antagonists. The absorption spectrum of the protein in the presence of thiamin exhibited significant hypochromism at the 278 nm band, indicating the involvement of aromatic amino acid residues of the protein, during its binding to the ligand. The protein cross-reacted with the monospecific antiserum to egg-white thiamin-binding protein, showing thereby that thiamin-binding proteins present in chicken egg yolk and white are the products of the same structural gene.     

Relationship between biotin-binding proteins from chicken plasma and egg yolk.

The plasma of laying hens contains a specific biotin-binding protein that appears to be identical with an egg-yolk biotin-binding protein. Both proteins are saturated with biotin and require elevated temperatures to effect the exchange of [14C]biotin for the protein-bound vitamin. The heat-exchange curve in each case is the same and differs sharply from that of avidin, the egg-white biotin-binding protein. On Sephadex G-100 gel filtration, plasma and yolk biotin-binding proteins were each eluted slightly ahead of avidin (mol.wt. 68,000), suggesting that they are of similar molecular weight. Plasma and yolk biotin-binding proteins required the same ionic strength to be eluted from a phosphocellulose ion-exchange column. Both the plasma and yolk biotin-binding proteins had a pI of 5; avidin has a pI of 10. Plasma biotin-binding protein cross-reacted with antiserum to yolk biotin-binding protein and showed a precipitin line of identity with purified yolk biotin-binding protein. It is suggested that biotin-binding plays an important role in mediating the transport of the vitamin from the bloodstream to the developing oocyte.