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  • insulin superfamily  (2)
  • Alkaline sizing  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Synthesis of bombyxin-IV, an insulin superfamily peptide from the silkworm,Bombyx mori, by stepwise and selective formation of three disulfide Bridges (1992)
    Springer
    The protein journal 11 (1992), S. 1-12 
    Details
    ISSN: 1573-4943
    Keywords: Prothoracicotropic hormone ; insect neuropeptide ; insulin superfamily ; peptide synthesis ; selective formation of disulfide bridges
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We report the synthesis of bombyxin-IV, a disulfide-linked, heterodimeric, insulin superfamily peptide from the silkworm,Bombyx mori. The two chains (A- and B-chains) were synthesized separately by the solid-phase method using fluoren-9-ylmethoxycarbonyl (Fmoc) group as a protecting group for α-amino group. Three disulfide bonds were bridged step by step (A6–A11, A20–B22, and A7–B10) in a good yield. Synthetic bombyxin-IV was identical with natural one with regard to the retention time on a reversed-phase column and the molecular weight measured by mass spectrometry. Circular dichroism (CD) spectrum of the synthetic bombyxin-IV was very similar to that of the natural one. The specific activity of synthetic bombyxin-IV is equal to that of natural one (0.1 ng/Samia unit). These results suggest that the synthetic bombyxin-IV has the tertiary structure identical with the natural peptide. Our method developed for synthesis of bombyxin-IV would be generally applicable to the synthesis of insulin-like heterodimeric peptides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025086
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  • 2
    Electronic Resource
    Electronic Resource
    Determination of disulfide bond arrangement in bombyxin-IV, an insulin superfamily peptide from the silkworm,Bombyx mori, by combination of thermolysin digestion of natural peptide and selective synthesis of disulfide bond isomers (1992)
    Springer
    The protein journal 11 (1992), S. 13-20 
    Details
    ISSN: 1573-4943
    Keywords: Disulfide bond ; insect neuropeptide ; insulin superfamily ; peptide synthesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The mode of disulfide linkages in bombyxin-IV, an insulin superfamily peptide consisting of A- and B-chains, was determined as A6–A11, A7–B10, and A20–B22. An intermolecular bond of A20–B22 was identified by sequencing and mass spectrometric analysis of the fragments generated by thermolysin digestion of natural bombyxin-IV. The mode of the remaining two bridges was determined by chemical and selective synthesis of three possible disulfide bond isomers of bombyxin-IV. A- and B-chains were synthesized by solid-phase method, and three disulfide bonds were bridged stepwise and in a fully controlled manner. Retention time on reversed-phase high-performance liquid chromatography (HPLC), thermolysin digests, and biological activity of the synthetic [A6–A11, A7–B10, A20–B22-cystine]-bombyxin-IV revealed that it was identical with the natural bombyxin-IV. Two other isomers with respect to disulfide bond arrangement, [A6–A7, A11–B10, A20–B22-cystine]- and [A6–B10, A7–A11, A20–B22-cystine]-bombyxin-IVs, were distinguishable from the natural one by use of HPLC, thermolysin digestion, and bioassay.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01025087
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  • 3
    Electronic Resource
    Electronic Resource
    Retention behavior of size and aluminum components on handsheets in rosin-ester size/alum systems (1999)
    Springer
    Journal of wood science 45 (1999), S. 46-52 
    Details
    ISSN: 1611-4663
    Keywords: Rosin-ester size ; Aluminum sulfate ; Retention ; Alkaline sizing ; Paper
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Anionic emulsion sizes consisting of rosin triglyceride esters and partly fortified rosin acids (i.e., rosin-ester sizes), have recently been used as internal sizes for alkaline papermaking. In this study, handsheets were prepared from pulp suspensions with alum and a rosin-ester size under various conditions, and sizing degree and size and aluminum contents of the handsheets were determined. Aluminum compounds originating from alum added to the pulp suspensions behave as retention aids of the rosin-ester size even in alkaline papermaking under limited conditions. Carboxyl groups in pulp are the primary retention sites of aluminum compounds in pulp suspensions. They form cationic sites on pulp fibers, and thus the anionic size emulsion particles are adsorbed on pulp fibers by electrostatic interactions. However, the cationic charges of aluminum compounds on pulp fibers decrease and finally disappear completely with the lapse of time after the alum addition by forming ionic bonds between the cationic sites and OH− ions. Thus, pH values of the pulp suspensions and timing of the size addition strongly influence the retention values of the rosin-ester size and the resultant sizing features.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00579523
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