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Chain Chinese hamster ovary

Manya, H., et al. (2000). Comparative study of the asparagine-linked sugar chains of human lipocalin-type prostaglandin D synthase purified from urine and amniotic fluid, and recombinantly expressed in Chinese hamster ovary cells. [Pg.382]

It is likely that the predominantly positively charged amino acids of TAT and other CPPs will interact with anionic components on the surface of the cell membrane (85). This idea is supported by the observation that cell association with CPP liposomes in glycosaminoglycan-deficient Chinese hamster ovary (CHO) cells is greatly reduced and is competitively inhibited by the presence of heparin (88,93). Furthermore, the removal of the heparan sulfate chains by the action of glycosaminoglycan lyase also suppressed the transduction of the TAT protein (94). [Pg.302]

Stevens VL, Nimkar S, Jamison WC, Liotta DC, Merrill AJJr (1990) Characteristics of the growth inhibition and cytotoxidty of long-chain (sphingoid) bases for Chinese hamster ovary cells evidence for an involvement of protein kinase C. Bio-chim Biophys Acta 1051 37-45... [Pg.91]

A. General description Interferon beta-la is produced by Chinese hamster ovary (CHO) cells into which the human interferon beta gene has been introduced. The amino-acid sequence of the recombinant protein produced by these cells is identical to naturally occurring interferon beta. Interferon beta-la is a single-chain glycosylated polypeptide, 166 amino-acid residues in length, with an approximate molecular weight of 22.5 kDa. [Pg.194]

Other mutants of Chinese-hamster ovary-cells having decreased amounts of lipid-linked oligosaccharides are known, although they are less well characterized. G-Protein of vesicular stomatitis virus grown in one of these mutants appeared to contain fewer, but full-sized rather than truncated, oligosaccharide side-chains. There may be insufficient amounts of oligosaccharide precursor available for transfer to nascent glycoproteins.172... [Pg.313]

MPO is a covalently linked dimeric glycoprotein of Mr 140 kDa comprised of 745 amino acids. MPO consists of three different isoenzyme forms termed a, b, and c. The natme of the chemical differences between these isoforms is not fiilly understood, and only isoform c has been crystallized. Catalytically active recombinant human MPO has been expressed in Chinese hamster ovary cells. However, incomplete posttranslational processing of the recombinant enzyme yields a monomeric form of the enzyme consisting of a single polypeptide chain of Mr 84 kDa with altered carbohydrate content. ... [Pg.1948]

C31. Conradt, H. S., Nimtz, M., Dittmar, K. E., Lindenmaier, W., Hoppe, J., and Hauser, H. Expression of human interleukin-2 in recombinant baby hamster kidney, Ltk-, and Chinese hamster ovary cells. Structure of O- linked carbohydrate chains and their location within the polypeptide. J. Biol. Chem. 264, 17368-17373 (1989). [Pg.60]

To date, commercial antibody expression exclusively uses mammalian cell line expression. These mammalian cell lines have expression cassettes for the antibody heavy and light chain stably integrated into the host cell chromosome. The most commonly used cell lines are derived from Chinese hamster ovary (CHO) cells. About half the approved antibody therapeutics are made in CHO cell lines. The dihydrofolate reductase (dhfr) gene is used as a selectable marker owing to the development of CHO cell lines that are deficient for dhfr genes such as CHO DG44 and CHO... [Pg.435]

Ridgvray ND, Meriiam DL. Metabolism of short-chain ceramide and dihydroceramide analogues in Chinese hamster ovary (CHO) cells. Biochim Biophys Acta 1256(1995) 57-70. [Pg.384]

Currently, it is standard procedure to develop ion channel-specific antibodies for immunocytochemistry, to perform Western and Northern blot analyses, ion channel in situ hybridization, or reverse transcription polymerase chain reaction (RT-PCR). The introduction of the single-cell RT-PCR in combination with the patch-clamp method in the 1990s made it possible to identify gene transcripts and to correlate them with functional data for the same individual cell. Finally, one of the most powerful cell biological techniques in the study of ion channels is based on artificial expression systems such as microinjection of mRNA encoding channel subunits into Xenopus oocytes and selective expression of native ion channels or with different subunit composition (e.g., Ky channel subunits). Because the Xenopus oocytes are large, they are a perfect model to study artificially expressed channels. Another good model for artificial ion channel expression is the Chinese hamster ovary (CHO) cell line. [Pg.414]

Takeuchi, M. et al. Relationship between sugar chain structure and biological activity of recombinant human erythropoietin produced in Chinese hamster ovary cells. Proc Natl Acad Sci USA, 86, 7819, 1989. [Pg.290]

In the Chinese hamster ovary cell line ts20, containing a thermosensitive ubiquitin-activating enzyme, El, Sachse et al. (2002) showed that this coat is predominantly present on early endosomes and has a characteristic bilayered appearance in the electron microscope. The coat contains clathrin heavy as well as light chain, but lacks the adaptor complexes API, AP2, and AP3, by which it differs from clathrin coats on endocytic vesicles and recycling endosomes. The coat is insensitive to short incubations with brefeldin A, but disappears in the presence of the phosphatidylinositol 3-kinase inhibitor wortmannin. [Pg.239]

Dibutyryl cAMP applied to Chinese hamster ovary cells in culture causes an increase in the number of microtubules per unit volume of cytoplasm (Porter et al., 1974). Microtubules end on microtubule organizing centers. A microtubule-associated protein, tau, will facilitate the initiation of tubulin polymerization and its subsequent elongation (Witman et al., 1976). The a chain of tubulin can be acted on by the enzyme tyrosyltubulin ligase, so as to add tyrosine, phenylalanine, or 3,4-dihydroxyphenylalanine to the C-terminus (Deanin and Gordon, 1976). [Pg.281]

Hokke,C.H.,Bergwerff,A.A.,VanDedem,G.W.K.,etfl/. (1995) Structural analysis of the sialylated N- and O-linked carbohydrate chains of recombinant human erythropoietin expressed in Chinese hamster ovary cells. Sialylation patterns and branch location of dimeric N-acetyllactosamine units. European Journal of Biochemistry, 228, 981-1008. [Pg.259]


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See also in sourсe #XX -- [ Pg.65 , Pg.98 ]




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