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C Crone J Frokjaer-Jensen JJ Friedman O Christensen 《The Journal of general physiology》1978,71(2):195-220
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Prolonged receptivity to the male and the fate of spermatozoa in the female black mastiff bat, Molossus ater 总被引:2,自引:0,他引:2
J J Rasweiler 《Journal of reproduction and fertility》1987,79(2):643-654
Observations were made on the reproductive biology of black mastiff bats maintained in a laboratory colony. Many of the females were inseminated within 24 h after the introduction of the males, and most exhibited a period of 10-50 days during which spermatozoa were present in their vaginal smears almost every day. The frequency of sperm-positive smears began to fall off around the time of implantation, but some smears taken much later in pregnancy were positive. The extent to which spermatozoa in the smears came from reservoirs in the female tract could not be thoroughly investigated, but evidence was obtained that the females have more than a limited period of oestrus. Female courtship behaviour and new copulations were sometimes observed many days after the start of the breeding activity. Also, histological studies of the reproductive tracts of females which had recently mated revealed that many were not in a periovulatory condition. Intact spermatozoa were usually found in the uterine horns and distal oviducts of preovulatory bats and those carrying tubal ova. Spermatozoa were absent from the oviducts of animals bearing early uterine embryos, and were much less abundant in the uterine horns after the start of implantation. Many of the excess spermatozoa appeared to have been expelled into the upper cervix where phagocytic leucocytes were commonly observed in the lumen. Some sperm components were also taken up by epithelial cells in the oviducts and uterine horns. 相似文献
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Lipoteichoic acid is an important microbe-associated molecular pattern of Lactobacillus rhamnosus GG
Claes Ingmar JJ Segers Marijke E Verhoeven Tine LA Dusselier Michiel Sels Bert F De Keersmaecker Sigrid CJ Vanderleyden Jos Lebeer Sarah 《Microbial cell factories》2012,11(1):1-8
Background
Receptors with a single transmembrane (TM) domain are essential for the signal transduction across the cell membrane. NMR spectroscopy is a powerful tool to study structure of the single TM domain. The expression and purification of a TM domain in Escherichia coli (E.coli) is challenging due to its small molecular weight. Although ketosteroid isomerase (KSI) is a commonly used affinity tag for expression and purification of short peptides, KSI tag needs to be removed with the toxic reagent cyanogen bromide (CNBr).Result
The purification of the TM domain of p75 neurotrophin receptor using a KSI tag with the introduction of a thrombin cleavage site is described herein. The recombinant fusion protein was refolded into micelles and was cleaved with thrombin. Studies showed that purified protein could be used for structural study using NMR spectroscopy.Conclusions
These results provide another strategy for obtaining a single TM domain for structural studies without using toxic chemical digestion or acid to remove the fusion tag. The purified TM domain of p75 neurotrophin receptor will be useful for structural studies. 相似文献10.