LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 3 of total 3

Search options

  1. Article: Simultaneous small-angle neutron scattering and Fourier transform infrared spectroscopic measurements on cocrystals of syndiotactic polystyrene with polyethylene glycol dimethyl ethers.

    Kaneko, Fumitoshi / Seto, Naoki / Sato, Shuma / Radulescu, Aurel / Schiavone, Maria Maddalena / Allgaier, Jürgen / Ute, Koichi

    Journal of applied crystallography

    2016  Volume 49, Issue Pt 5, Page(s) 1420–1427

    Abstract: Syndiotactic polystyrene (sPS) is a crystalline polymer which has a unique property; it is able to form cocrystals with a wide range of chemical compounds, in which the guest molecules are confined in the vacancies of the host sPS crystalline region. ... ...

    Abstract Syndiotactic polystyrene (sPS) is a crystalline polymer which has a unique property; it is able to form cocrystals with a wide range of chemical compounds, in which the guest molecules are confined in the vacancies of the host sPS crystalline region. Recently, it has been found that even polyethylene glycol oligomers with a molecular weight of more than several hundreds can be introduced into the sPS crystalline region. It is quite important to know how such a long-chain molecule is stored in the host sPS lattice. To tackle this issue, a new simultaneous measurement method combing small-angle neutron scattering and Fourier transform infrared spectroscopy (SANS/FTIR), which has been recently developed by the authors, was applied to an sPS cocrystal with polyethylene glycol dimethyl ether with a molecular weight of 500 (PEGDME500). The temperature-dependent changes of the SANS profile and FTIR spectrum were followed from room temperature up to 413 K for a one-dimensionally oriented SANS/PEGDME500 cocrystal sample. The intensity of the reflections due to the stacking of crystalline lamellae showed a significant temperature dependence. The two-dimensional pattern in the high
    Language English
    Publishing date 2016-08-04
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2020879-0
    ISSN 1600-5767 ; 0021-8898
    ISSN (online) 1600-5767
    ISSN 0021-8898
    DOI 10.1107/S160057671601178X
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article: Construction and Characterization of Single-chain Antibodies Against Human Insulin-like Growth Factor-I Receptor from Hybridomas Producing 1H7 or 3B7 Monoclonal Antibody

    Kusada, Yu / Morizono, Toru / Matsumoto-Takasaki, Ayano / Sakai, Keiko / Sato, Shuma / Asanuma, Hideki / Takayanagi, Atsushi / Fujita-Yamaguchi, Yoko

    Journal of biochemistry. 2008 Jan., v. 143, no. 1

    2008  

    Abstract: Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG₁ Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast ... ...

    Abstract Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG₁ Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast cancer growth in vitro and in vivo [Li et al. (2000) Cancer Immunol. Immunother. 49, 243; Sachdev et al. (2003) Cancer Res. 63, 627]. Various types of scFvs from hybridomas producing 1H7 or 3B7 mAb were constructed using conventional phage display technology to further characterize the specificity and affinity of anti-IGF-IR mAbs. Binding studies performed using either phage antibodies or soluble scFv proteins to IGF-IR or insulin receptor (IR) and IGF-IR pre-incubated with mAbs suggested that (i) 1H7 and 3B7 bind to IGF-IR but do not bind to its structurally related IR, (ii) either the VL-VH or VH-VL sequence order does not apparently affect specificity for IGF-IR and (iii) 1H7 and 3B7 bind the independent epitopes, located in or near the N-terminal (440-514) and C-terminal (62-184) domains of the α subunit, respectively. This study not only revealed new information on binding regions for two anti-IGF-IR mAbs, but also provided the scFv genes as tools for further manipulation of the affinity or development of new IGF-IR-targeted cancer therapeutics.
    Language English
    Dates of publication 2008-01
    Size p. 9-19.
    Publishing place Japanese Biochemical Society
    Document type Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 80/714: Show issues
    Z 6.2: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  3. Article: Construction and characterization of single-chain antibodies against human insulin-like growth factor-I receptor from hybridomas producing 1H7 or 3B7 monoclonal antibody.

    Kusada, Yu / Morizono, Toru / Matsumoto-Takasaki, Ayano / Sakai, Keiko / Sato, Shuma / Asanuma, Hideki / Takayanagi, Atsushi / Fujita-Yamaguchi, Yoko

    Journal of biochemistry

    2008  Volume 143, Issue 1, Page(s) 9–19

    Abstract: Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG(1) Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast ... ...

    Abstract Recombinant antibody consisting of the single-chain variable fragment (scFv) of 1H7 monoclonal antibody against insulin-like growth factor-I receptor (IGF-IR) and human IgG(1) Fc domain, scFv-Fc, has been found to exhibit inhibitory effects on breast cancer growth in vitro and in vivo [Li et al. (2000) Cancer Immunol. Immunother. 49, 243; Sachdev et al. (2003) Cancer Res. 63, 627]. Various types of scFvs from hybridomas producing 1H7 or 3B7 mAb were constructed using conventional phage display technology to further characterize the specificity and affinity of anti-IGF-IR mAbs. Binding studies performed using either phage antibodies or soluble scFv proteins to IGF-IR or insulin receptor (IR) and IGF-IR pre-incubated with mAbs suggested that (i) 1H7 and 3B7 bind to IGF-IR but do not bind to its structurally related IR, (ii) either the VL-VH or VH-VL sequence order does not apparently affect specificity for IGF-IR and (iii) 1H7 and 3B7 bind the independent epitopes, located in or near the N-terminal (440-514) and C-terminal (62-184) domains of the alpha subunit, respectively. This study not only revealed new information on binding regions for two anti-IGF-IR mAbs, but also provided the scFv genes as tools for further manipulation of the affinity or development of new IGF-IR-targeted cancer therapeutics.
    MeSH term(s) Antibodies, Monoclonal/biosynthesis ; Antibodies, Monoclonal/immunology ; Antibody Specificity ; Epitopes/immunology ; Humans ; Hybridomas/immunology ; Immunoglobulin Variable Region/genetics ; Immunoglobulin Variable Region/immunology ; Immunoglobulin Variable Region/metabolism ; Peptide Library ; Receptor, IGF Type 1/chemistry ; Receptor, IGF Type 1/immunology
    Chemical Substances Antibodies, Monoclonal ; Epitopes ; Immunoglobulin Variable Region ; Peptide Library ; Receptor, IGF Type 1 (EC 2.7.10.1)
    Language English
    Publishing date 2008-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvm192
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.202: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top