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Bombyx mori silkworm

Z. E. Jouni and M. Wells, Purification of a carotenoid-binding protein from the midgut of the silkworm, Bombyx mori, Ann. N. Y. Acad. Sci. 691 (1993) 210-212. [Pg.378]

Imamura, M., Nakai, J., Inoue, S., Quan, G. X., Kanda, T., and Tamura, T. 2003. Targeted gene expression using the GAL4/UAS system in the silkworm Bombyx mori. Genetics, 165(3) 1329-1340. [Pg.522]

Jouni, Z. E. and Wells, M. A. 1996. Purification and partial characterization of a lutein-binding protein from the midgut of the silkworm Bombyx mori. J. Biol. Chem., 271(25) 14722-14726. [Pg.522]

Suetsugu, Y., Minami, H., Shimomura, M. et al. 2007. End-sequencing and characterization of silkworm (Bombyx mori) bacterial artificial chromosome libraries. BMC Genomics, 8 314. [Pg.522]

Tabunoki, H., Higurashi, S., Ninagi, O. et al. 2004. A carotenoid-binding protein (CBP) plays a crucial role in cocoon pigmentation of silkworm (Bombyx mori) larvae. FEBS Lett., 567(2-3) 175-178. [Pg.523]

Tamura, T., Thibert, C., Royer, C. et al. 2000. Germline transformation of the silkworm Bombyx mori L. using apiggyBac transposon-derived vector. Nat. Biotechnol., 18(1) 81—84. [Pg.523]

Uchino, K., Imamura, M., Sezutsu, H. et al. 2006. Evaluating promoter sequences for trapping an enhancer activity in the silkworm Bombyx mori. J. Insect Biotechnol. Sericology, 75 89-97. [Pg.523]

Yamamoto, K., Narukawa, J., Kadono-Okuda, K. et al. 2006. Construction of a single nucleotide polymorphism linkage map for the silkworm, Bombyx mori, based on bacterial artificial chromosome end sequences. Genetics, 173(1) 151—161. [Pg.523]

The first spinning experiments were performed with dissolved raw silk of the silkworm Bombyx mori [31] and the golden orb-weaver Nephila clavipes [32]. For this purpose a minimized wet-spinning apparatus was constructed [31]. The apparatus was capable of spinning fibers from solutions containing 10 mg of soluble protein. [Pg.174]

Silk fibers or monolayers of silk proteins have a number of potential biomedical applications. Biocompatibility tests have been carried out with scaffolds of fibers or solubilized silk proteins from the silkworm Bombyx mori (for review see Ref. [38]). Some biocompatibility problems have been reported, but this was probably due to contamination with residual sericin. More recent studies with well-defined silkworm silk fibers and films suggest that the core fibroin fibers show in vivo and in vivo biocompatibility that is comparable to other biomaterials, such as polyactic acid and collagen. Altmann et al. [39] showed that a silk-fiber matrix obtained from properly processed natural silkworm fibers is a suitable material for the attachment, expansion and differentiation of adult human progenitor bone marrow stromal cells. Also, the direct inflammatory potential of silkworm silk was studied using an in vitro system [40]. The authors claimed that their silk fibers were mostly immunologically inert in short and long term culture with murine macrophage cells. [Pg.175]

Yusifov, N.I., A.M. Kuzin, F.A. Agaev, and S.G. Alieva. 1990. The effect of low level ionizing radiation on embryogenesis of silkworm, Bombyx mori L. Radiation Environ. Biophys. 29 323-327. [Pg.1753]

The sex pheromone communication system basically involves the release of specific chemicals from a pheromone producer (emitter), the transmission of these chemicals in the environment to a receiver, and the processing of these signals to mediate appropriate behavioral responses in the receiver. The chemicals transmitted downwind have been the most obvious targets for characterization. The code was first broken with the publication in 1959 (3) of the sex pheromone for the domesticated silkworm Bombyx mori after extraction of a half million female silkworm pheromone glands and 30 years of classical chemical analyses. The pheromone was found to be (E10, Z12)-hexadecadien-l-ol, which was called bombykol. This work showed that there was nothing magical about the communication system, and chemists around the world were "attracted" to this area of research on insect pheromones. [Pg.115]

Iizuka, E. (1966). Mechanism of fibre formation by the silkworm Bombyx Mori. Biorheology 3, 141-152. [Pg.46]

Sirichaisit, J., Brookes, V. L., Young, R.J., and Vollrath, F. (2003). Analysis of structure/ property relationships in silkworm (Bombyx mori) and spider dragline (Nephila edulis) silks using Raman spectroscopy. Biomacromolecules 4, 387-394. [Pg.50]

Pharmacologically active allenic steroids have already been examined intensively for about 30 years [5], Thus, the only naturally occurring allenic steroid 107 had been synthesized 3 years before its isolation from Callyspongia diffusa and it had been identified as an inhibitor of the sterol biosynthesis of the silkworm Bombyx mori (Scheme 18.34) [86d], At this early stage, allenic 3-oxo-5,10-secosteroids of type 108 were also used for the irreversible inhibition of ketosteroid isomerases in bacteria, assuming that their activity is probably caused by Michael addition of a nucleophilic amino acid side chain of the enzyme at the 5-position of the steroid [103, 104]. Since this activity is also observed in the corresponding /3,y-acetylenic ketones, it can be rationalized that the latter are converted in vivo into the allenic steroids 108 by enzymatic isomerization [104, 105],... [Pg.1019]

Ommochromes belong to the naturally occurring pigments present in many members of the animal kingdom mainly in insects. Their presence in the central nervous system of the silkworm Bombyx mori was proved by using cellulose and silica stationary phases. The Rp values of standards and the isolated pigments are compiled in Tables 2.107 and 2.108. [Pg.322]

H. Sawada, M. Nakagoshi, K. Mase and T. Yamamoto, Occurrence of ommochrome-containg pigment granules in the central nervous system of the silkworm Bombyx mori. Comp. Biochem. Physiol. Part B 125 (2000) 421 —428. [Pg.366]

Asano N, Yamashita T, Yasuda K, Ikeda K, Kizu H, Kameda Y, kato A, Nash RJ, Lee HS, Ryu KS. (2001) Polyhydroxylated alkaloids isolated from mulberry trees Moms alba L.) and silkworms Bombyx mori L.). J Agric Food Chem 49 4208-4213. [Pg.584]

The early work focused on a particular silkworm, Bombyx mori, that lives on mulberry bushes. There are other silkworms each with its own special properties, but in general most silk is still derived from the original strain of silkworm. Crystalline silk fiber is about four times stronger than steel on a weight basis. [Pg.309]

The silkworm, Bombyx mori (Bombycidae), contains in various body parts simple alkylamines, tryptophan metabolites, and pteridines (Tables V, VI, and VIII). One of the pteridines, violapterin (78), is synthesized from isoxanthopterin (67) by isoxanthopterin deaminase, occurring in the larvae and adults, and is stored in situ in the larval and adult integument (80). In addition, sepiapterin deaminase in the integument of the lemon mutant silkworm catalyzes the deamination of sepiapterin (81) to 7,8-dihydro-6-lactyllumazine (79) (81). [Pg.201]

Figure 2. A molting cycle failure of the silkworm, Bombyx mori, caused by ingestion of the crude methanol extract of Ajuga remota root. The insect underwent normal apolysis, but failed to complete ecdysis. Thus, it could not remove its head capsule or its trunk exuviae. Magnification X11. Figure 2. A molting cycle failure of the silkworm, Bombyx mori, caused by ingestion of the crude methanol extract of Ajuga remota root. The insect underwent normal apolysis, but failed to complete ecdysis. Thus, it could not remove its head capsule or its trunk exuviae. Magnification X11.
Adipokinetic hormones control metabolism of insects during long-distance flight.359 363 In the migratory locust these hormones consist of a pair of related octapeptides and a decapeptide (Table 30-5). The hormones stimulate triacylglycerol lipase in the insects fat bodies, induce release of carbohydrates from body stores, and affect many other aspects of metabolism.363 Insects also have hormones of the insulin family, proteins consisting of disulfide-linked A and B chains as in insulin. The silkworm Bombyx mori has 38 genes for the insulinlike bombyxins, which are synthesized in the brain.364... [Pg.1760]

Konno, K., Hirayama, C., and Shinbo, H., Unusually high concentration of free glycine in the midgut content of the silkworm, Bombyx mori, and other lepidopteran larvae, Comp. Biochem. Physiol., 115A, 229, 1996. [Pg.410]

Kitamura A., Nagasawa H., Kataoka H., Inoue T., Matsumoto S., Ando T. and Suzuki A. (1989) Amino acid sequence of pheromone biosynthesis activating neuropeptide (PB AN) of the silkworm, Bombyx mori. Biochem. Biophys. Res. Commun. 163, 520-526. [Pg.15]

Yoshiga T., Okano K., Mita K., Shimada T. and Matsomoto S. (2000) cDNA cloning of acyl-CoA desaturase homologs in the silkworm, Bombyx mori. Gene 246, 339-345. [Pg.106]

Fonagy A., Yokoyama N., Ozawa R., Okano K., Tatsuki S., Maeda S. and Matsumoto S. (1999) Involvement of calcineurin in the signal transduction of PBAN in the silkworm, Bombyx mori (Lepidoptera). Comp. Biochem. Physiol. B Biochem. Mol. Biol. 124,51-60. [Pg.128]

Ichikawa T., Hasegawa K., Shimizu I., Katsuno K., Kataoka H. and Suzuki A. (1995) Structure of neurosecretory cells with immunoreactive diapause hormone and pheromone biosynthesis activating neuropeptide in the silkworm, Bombyx mori. Zool. Sci. 12, 703-712. [Pg.129]

Imai K., Konno T., Nakazawa Y., Komiya T., Isobe M., Koga K., Goto T., Yaginuma T., Sakakibara K. and Hasegawa K., el al. (1991) Isolation and structure of diapause hormone of the silkworm, Bombyx mori. Proc. Japan Acad. 67(B), 98-101. [Pg.130]

Amino acid sequence of pheromone-biosynthesis-activating neuropeptide (PB AN) of the silkworm, Bombyx mori. Biochem. Biophys. Res. Commun. 163, 520-526. [Pg.131]

Sato Y., Oguchi M., Menjo N., Imai K., Saito H., Ikeda M., Isobe M. and Yamashita O. (1993) Precursor polyprotein for multiple neuropeptides secreted from the suboesophageal ganglion of the silkworm Bombyx mori characterization of the cDNA encoding the diapause hormone precursor and identification of additional peptides. Proc. Natl. Acad. Sci. USA 90, 3251-3255. [Pg.135]

Sato Y., Ikeda M., Yamashita O. (1994) Neurosecretory cells expressing the gene for common precursor for diapause hormone and pheromone biosynthesis activating neuropeptide in the subesophageal ganglion of the silkworm, Bombyx mori. Gen. Comp. Endocrin. 96, 27-36. [Pg.135]

Shimizu, S., Tsuchitani, Y., and Matsumoto, T. (1993). Production of an extracellular protease by Beauveria bassiana in the haemolymph of the silkworm, Bombyx mori, Letters in Applied Microbiology, 16, 291-294. [Pg.296]


See other pages where Bombyx mori silkworm is mentioned: [Pg.294]    [Pg.238]    [Pg.512]    [Pg.522]    [Pg.523]    [Pg.173]    [Pg.1705]    [Pg.181]    [Pg.602]    [Pg.1751]    [Pg.294]    [Pg.291]   
See also in sourсe #XX -- [ Pg.1776 , Pg.1777 ]

See also in sourсe #XX -- [ Pg.1776 , Pg.1777 ]

See also in sourсe #XX -- [ Pg.384 ]




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