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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    The @journal of physical chemistry 〈Washington, DC〉 89 (1985), S. 862-867 
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-8935
    Keywords: Poly(imide siloxane) film ; True interfacial adhesion ; Morphology ; Critical surface tension ; Phase separation ; Alloy-42 leadframe ; Peel strength
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract The effect of surface characteristics and morphology of poly(imide siloxane) (PIS) on the true interfacial adhesion between PIS films and alloy-42 substrates was studied. The effect of the viscosity of PIS films and the surface treatment of deep UV/O3 (d-UV/O3) on alloy-42 plates on the peel strength of PIS films/alloy-42 joints has also investigated. 3,3′,4,4′-benzophenone tetracarboxylic dianhydride/2,2′-bis[4-(3-aminophenoxy)phenyl]sulfone (BTDA/m-BAPS) based PIS films with α,ω-bis(3-aminopropyl)polydimethyl siloxane (APPS) molecular weight Mn = 996 g/mole (PIS9Siy) show two phases in all compositions and the linear dependence of the critical surface tension on the surface concentration of the silicon, [Sisurf], on the PIS films. The PIS films with the APPS Mn = 507 g/mole (PIS5Siy) or Mn = 715 g/mole (PIS7Siy) exhibit a morphology change from a homogeneous phase to an inhomogeneous phase starting at the mole ratio (y) of APPS/PIS = 2.7% and 1.1%, respectively. The curves of critical surface tension dependence on the [Sisurf] discontinue or deflect at these two compositions, respectively. The treatment of d-UV/O3 on alloy-42 plates improves the wetting on the alloy surface and promotes the peel strength between the PIS films and alloy-42 plates by a magnitude of ≥ 20%. These results show that the flowability of the same PIS films bonding at different temperatures significantly affects the bonding strength of the joints, but the flowability of different PIS films bonding at the same temperature, e.g. 400 °C, is not the key factor governing the bonding strength of the joints. The true interfacial adhesion of the PIS5Si0.6/alloy-42 joint is 80% higher than that of the unmodified BTDA/m-BAPS based polyimide film/alloy-42 joint. However, zero true interfacial adhesion is obtained between the PIS9Siy films and alloy-42 plates. The wetting kinetics experiment shows that the higher the siloxane content in the PIS, the higher the activation energy for the adhesive bonding process. Moreover, the phase sepration significantly increases the activation energy. The scanning electron micrographs of the peeled-off PIS film surfaces from the PIS/alloy-42 joints reveal the rougher surface morphology from the sample with the higher interfacial adhesion.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4943
    Keywords: γ-Crystallins ; shark lens ; polymerase chain reaction (PCR) ; multigene family ; phylogenetic tree
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract γ-Crystallin is a common lens protein of most vertebrate eye lenses and the major protein component in lenses of fishes and in many mammalian species during embryonic and neonatal stages. To facilitate the structural characterization of γ-crystallin possessing extensive charge heterogeneity, a cDNA mixture was constructed from the poly(A)+ mRNA isolated from shark eye lenses, and amplification by polymerase chain reaction (PCR) was carried out to obtain cDNAs encoding multiple shark γ-crystallins. Sequencing analysis of multiple positive clones containing PCR-amplified inserts revealed the presence of a multiplicity of isoforms in the γ-crystallin class of this cartilaginous fish. It was of interest to find that two shark cDNA sequences coexist, one encoding γ-crystallin (γM1) of high methionine content (15.5%) and the other encoding one (γM2) of low methionine content (5.1%), each corresponding to the major teleostean and mammalian γ-crystallins, respectively. Comparison of protein sequences encoded by these two shark cDNAs with published sequences of γ-crystallins from mouse, bovine, human, frog, and carp lenses indicated that there is about 61–80% sequence homology between different species of the piscine class, whereas only 47–66% is found between mammals and shark. A phylogenetic tree constructed on the basis of sequence divergence among various γ-crystallin cDNAs revealed the close relatedness between shark γM2-crystallin and mammalian γ-crystallins and that between shark γM1 and teleostean γ-crystallins. The results pointed to the fact that ancestral precursors of γ-crystallins were present in the sharp lens long before the appearance of modern-day mammalian and teleostean γ-crystallins.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4943
    Keywords: γ-Crystallin ; amphibian lens ; polymerase chain reaction (PCR) ; sequence comparison ; multigene family ; phylogenetic tree
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract γ-Crystallin is the major and most abundant lens protein present in the eye lens of lower vertebrates such as amphibian and piscine species. To facilitate structural characterization ofγ-crystallins isolated from the lens of the bullfrog (Rana catesbeiana), a cDNA mixture was synthesized from the poly(A)+mRNA isolated from fresh eye lenses. cDNA encodingγ-crystallin was then amplified using polymerase chain reaction (PCR) based on two primers designed according to the relatively conserved N- and C-terminal sequences of knownγ-crystallins from teleostean fishes. PCR-amplified product corresponding toγ-crystallin isoforms was obtained, which was then subcloned in pUC18 vector and transformed intoEscherichia coli strain JM109. Plasmids containing amplifiedγ-crystallin cDNAs were purified and prepared for nucleotide sequencing by the dideoxynucleotide chain-termination method. Sequencing several clones containing DNA inserts of about 0.54 kb revealed the presence of two isoforms with an open reading frame of 534 base pairs, covering twoγ-crystallins each with a deduced protein sequence of 177 amino acids including the translation-initiating methionine. Theseγ-crystallins of pI 6.364 and 6.366 contain a low-methionine content of 2.81%, in contrast to 11–16% obtained for thoseγ-crystallins with high-methionine content from most teleostean lenses. Pairwise sequence comparison of bullfrogγ-crystallins with those published sequences ofγ-crystallins from carp, shark,Xenopus and anotherRana frog, bovine, and human lenses indicates that there is only 46–63% sequence similarity among these species, revealing that amphibians possess a very complex and heterogeneous group ofγ-crystallins even from closely related species ofRana frogs. The sequence analysis and comparison of various isoforms of the frogγ-crystallin family provide a firm basis for identifying these lens proteins as members of a multigene family more complex than that reported for mammalianγ-crystallins.
    Type of Medium: Electronic Resource
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