Coturnix

About: Coturnix is a research topic. Over the lifetime, 953 publications have been published within this topic receiving 23305 citations.

Cloning of a novel ovalbumin gene from quail oviduct and its heterologous expression in Pichia pastoris.

Abstract: An ovalbumin gene was cloned from Chinese quail (Coturnix coturnix) oviduct by RT-PCR and then inserted into the P. pastoris genome under the control of the methanol inducible 5' alcohol oxidase (AOX) promoter. The recombinant P. pastoris strain was demonstrated to be able to efficiently secrete quail ovalbumin by ELISA analysis using a polyclonal antibody raised against quail ovalbumin. The results showed that induction by 0.75% methanol for 48 h led to the synthesis of secreted quail ovalbumin up to a yield of 5.45 g l(-1). The recombinant ovalbumin was further purified into homogeneity through ion exchange and gel filtration chromatography and SDS-PAGE analysis revealed that, compared to natural ovalbumin, the recombinant ovalbumin could have been glycosylated to the similar extent by P. pastoris.

In vitro degradation of hexanitrohexaazaisowurtzitane (CL-20) by cytosolic enzymes of Japanese quail and the rabbit.

Abstract: Hexanitrohexaazaisowurtzitane (CL-20) is a polycyclic nitramine explosive and propellant, currently being considered as a potential replacement for existing cyclic nitramine explosives. Earlier studies have provided evidence suggestive of adverse liver effects in adult Coturnix spp. exposed to CL-20, yet analysis of tissue samples (plasma, liver, brain, heart, or spleen) indicated that CL-20 was not detectable in these treated animals. The present study was conducted to identify and purify the enzymes capable of CL-20 biotransformation. Results indicate that the hepatic biotransformation of CL-20 in vitro was inhibited by ethacrynic acid (93%) and by the glutathione (GSH) analogue S-octylglutathione (80%), suggesting the involvement of glutathione-S-transferase (GST). Partially purified cytosolic α- and μ-type GST (requiring presence of GSH as a cofactor) from quail and rabbit liver was capable of CL-20 biotransformation. The degradation of CL-20 (0.30 ± 0.05 and 0.40 ± 0.02 nmol/min/mg protein for quail and rabbit, respectively) was accompanied with the formation of nitrite and consumption of GSH. Using liquid chromatography/mass spectrometry, we detected two intermediates, that is, open-ring, monodenitrated GSH–conjugated CL-20 biotransformation product with the same deprotonated molecular mass ion at 699 Da, suggesting isomeric forms of the intermediate metabolites. Identity of the conjugated metabolites was confirmed by using ring-labeled [15N]CL-20 and the nitro group–labeled [15NO2]CL-20. These data suggest that the in vitro biotransformation of CL-20 by GST under the conditions tested may be a key initial step in the in vivo degradation of CL-20 in the quail and resulted in the formation of more biologically reactive intermediates than the parent compound. These data will aid in our understanding of the biotransformation processes of CL-20 in vivo.

Comparison of the rates of muscle protein metabolism between the domestic and the wild coturnix quail.

Abstract: Skeletal muscle functions in controlling movement and is the major organ of protein deposition and for the provision of amino acids in protein metabolism. Therefore, it is very interesting to find out if there is a relationship between muscle protein metabolism and biological function. There is some evidence of a genetic basis for muscle protein metabolism (Maeda et al., 1984, 1986, 1987a, b, 1990). Maeda et al. (1984, 1986) reported that muscle protein turnover rate differed among breeding stocks, i.e., between modern improved stocks and unimproved native chicken stocks, or among lines selected for body size. These differences in protein metabolism rate among stocks mean that selective breeding resulted in genetic differentiation in metabolic adaptation resulting in improvement. Almost all of the studies on protein metabolism have been conducted using domesticated animals. There is no report on protein metabolism of wild species. Probably, protein metabolism in wild animals and wild species differs from that in domesticated stocks. The coturnix quail is a good experimental animal for studies of muscle protein metabolism because the level of excretion of N'-methylhistidine (N'-MH) is valid as a measurement of muscle protein turnover rate. Fortunately, wild coturnix quail which migrate from Siberia to the islands of Japan every winter were captured. The present study was conducted to examine the difference in muscle

Photoinduced changes in subcellular structures of the retinal pigment epithelium from the Japanese quail Coturnix japonica.

Abstract: Fifteen-week-old sexually mature female Japanese quails (Coturnix japonica) grown under various lighting conditions were used in the study. It was found that the number of mitochondria and phagosomes was increased by 1.5-fold in the retinal pigment epithelium from birds reared for 95 days under blue light (440-470 nm) vs. reduced blue light component conditions. Also, it was found that egg production was increased by 15% in birds reared under blue light compared to other lightning conditions. Thus, we concluded that blue light conditions resulted in elevating metabolic activity and accelerating pace of life in Japanese quails. It is assumed that the blue light-induced effects are probably due to inhibition of melatonin synthesis.

Vagal influence on respiratory and cardiac responses of coturnix quail to heat

Abstract: Measurements of heart rate, respiratory rate, surface temperature (Ts) and rectal temperature (Tre) of mature Coturnix quail were continuously recorded for 30 min at 25° and 38°C environmental temperatures. Ts and Tre increased to a maximum level within 16 and 20 min after exposure to the 38°C environment. Thermal panting was initiated after a 1.3°C rise in rectal temperature and 12 min of exposure to 38°C. Heart rate decreased consistently during the first 20 min at 38°C, then remained at the decreased level. The increase in heart rate at 38°C following atropine injection (0.1 mg/100 g body weight) and subsequent bilateral vagotomy indicated that the decrease in heart rate is the result of an increase in vagal tone and that both efferent and afferent vagi are involved in the decreased heart rate.