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  • Springer  (12,876)
  • MDPI Publishing  (1,195)
  • Public Library of Science (PLoS)
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  • 1
    Electronic Resource
    Electronic Resource
    Photoluminescence from ordered and disordered Si-SiGe superlattices (1996)
    Springer
    Optical and quantum electronics 28 (1996), S. 1295-1303 
    Details
    ISSN: 1572-817X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: Abstract Ordered (Ord-SL) and disordered (Dis-SL) Si-SiGe superlattices are grown using ultrahigh vacuum chemical vapour deposition (UHVCVD). The results of cross-sectional transmission electron microscopy (XTEM) and high-resolution double crystal x-ray diffraction (HRXRD) indicate that high quality Si-SiGe superlattices can be achieved. Well-defined band-edge excitonic luminescence is observed for the Si0.86Ge0.14-Si superlattice. Stronger phosoluminescence (PL) is observed for the Si-SiGe disordered superlattice compared with the corresponding Si-SiGe ordered superlattice. Furthermore, PL peak energy of the Dis-SL shifts to lower value with respect to the peak position of the corresponding Ord-SL. The stronger intensity of the no-phonon (NP) peak and the red shift of the PL peak are possibly a result of two probable mechanisms: (i) the tunnelling effect and (ii) the formation of localized states.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326202
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  • 2
    Electronic Resource
    Electronic Resource
    Application of recombinant rhodostomin in studying cell adhesion (1997)
    Springer
    Journal of biomedical science 4 (1997), S. 235-243 
    Details
    ISSN: 1423-0127
    Keywords: Kistrin ; Disintegrin ; Integrin ; Extracellular matrix ; Metastasis ; Bone marrow stromal cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Rhodostomin from venom ofAgkistrodon rhodostoma (also calledCalloselasma rhodostoma) contains 68 amino acid residues including 6 pairs of disulfide bonds and an arginine-glycine-aspartic acid (RGD) sequence at positions 49–51. It has been known as one of the strongest antagonists to platelet aggregation among the family termed disintegrin. In this review paper, in addition to introducing the characteristics of disintegrin and its related molecules, the advantages of using recombinant DNA technology to produce rhodostomin are described. The recombinant rhodostomin has been demonstrated to facilitate cell adhesion via interaction between the RGD motif of rhodostomin and integrins on the cell surface. This property allowed us to use the recombinant rhodostomin as an extracellular matrix to study cell adhesion and to distinguish attachment efficiency between two melanoma cell lines B16-F1 and B16-F10, the former is a low metastasis cell while the latter is a high metastasis cell. Furthermore, by using the recombinant rhodostomin as a substrate, osteoprogenitor-like cells are able to be selected and enriched within 3 days from rat bone marrow which contains a heterogeneous cell population. Finally, we show that the recombinant rhodostomin can be immobilized on beads and which serve as an affinity column to dissect cell-surface protein(s) binding to the RGD motif of rhodostomin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02253423
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  • 3
    Electronic Resource
    Electronic Resource
    Molecular analysis of survival motor neuron (SMN) and neuronal apoptosis inhibitory protein (NAIP) genes of spinal muscular atrophy patients and their parents (1997)
    Springer
    Human genetics 〈Berlin〉 100 (1997), S. 577-581 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have assayed deletions of two candidate genes for spinal muscular atrophy (SMA), the survival motor neuron (SMN) and neuronal apoptosis inhibitory protein (NAIP) genes, in 101 patients from 86 Chinese SMA families. Deletions of exons 7 and 8 of the telomeric SMN gene were detected in 100%, 78.6%, 96.6%, and 16.7%, in type I, II, III, and adult-onset SMA patients, respectively. Deletion of exon 7 only was found in eight type II and one type III patient. One type II patient did not have a deletion of either exon 7 or 8. The prevalence of deletions of exons 5 and 6 of the NAIP gene were 22.5% and 2.4% in type I and II SMA patients, respectively. We also examined four polymorphisms of SMN genes and found that there were only two, SMN-2 and CBCD541-2, in Chinese subjects. In our study, analysis of the ratio of the telomeric to centromeric portion (T/C ratio) of the SMN gene after enzyme digestion was performed to differentiate carriers, normals, and SMA patients. We found the T/C ratio of exon 7 of the SMN gene differed significantly among the three groups, and may be used for carrier analysis. An asymptomatic individual with homozygous deletion of exons 7 and 8 of the SMN gene showed no difference in microsatellite markers in the SMA-related 5q11.2–5q13.3. In conclusion, SMN deletion in clinically presumed child-onset SMA should be considered as confirmation of the diagnosis. However, adult-onset SMA, a heterogeneous disease with phenotypical similarities to child-onset SMA, may be caused by SMN or other gene(s).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050555
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  • 4
    Electronic Resource
    Electronic Resource
    The Structural Variations of ε-Amino Groups in Phospholipase A2 Enzymes from Naja naja atra and Bungarus Multicinctus Venoms (1997)
    Springer
    The protein journal 16 (1997), S. 133-137 
    Details
    ISSN: 1573-4943
    Keywords: Phospholipase A2 ; structural variations of side chains ; modification of lysine residues ; electrophoretic analysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Comparative studies on Naja naja atra phospholipase A2 (NNA-PLA2), Bungarus multicinctus phospholipase A2 (BM-PLA2), and their Lys-modified derivatives were made to assess the differences in the fine structures around the conserved Lys residues of PLA2 enzymes. It was found that the accessibility of Lys residues of PLA2 enzymes toward modified reagent, trinitrobenzene sulfonate, were not the same. Moreover, the extent of decrease in pI values of PLA2 enzymes that resulted from trinitrophenylation of lysine residues was different between NNA-PLA2 and BM-PLA2. The Lys-6 of BM-PLA2 mostly contributed to the positively charged character of the enzyme molecule, whereas the contribution of Lys-6 of NNA-PLA2 to its molecular charge was not notably different from other Lys residues. A linear relationship was observed by plotting the mobilities of PLA2 enzymes and their TNP derivatives against their pI values. However, native and Lys-modified NNA-PLA2 were not aligned with those of BM-PLA2 in the same line. Apparently the gross conformation of PLA2 enzymes was not notably perturbed by the modification of Lys residues, but the fine structure of NNA-PLA2 was not the same as that of BM-PLA2. These results indicate that the positioning of side chains of the conserved Lys residues in the two PLA2 enzymes is essentially different, and suggest that the variations in the fine structures of homologous proteins could be effectively explored by chemical modification studies and electrophoretic analysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026394118064
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  • 5
    Electronic Resource
    Electronic Resource
    Energy transfer from tryptophan residues of proteins to 8-anilinonaphthalene-1-sulfonate (1994)
    Springer
    The protein journal 13 (1994), S. 635-640 
    Details
    ISSN: 1573-4943
    Keywords: Trp fluorescence ; energy transfer ; 8-anilinonaphthalene sulfonate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The binding of the apolar fluorescent dye 8-anilinonaphthalene-1-sulfonate (ANS) to bovine serum albumin (BSA), phospholipase A2 (PLA2), ovalbumin, lysozyme, cobrotoxin and N-acetyltryptophanamide was used to assess the factors affecting the efficiency of energy transfer from Trp residues to the ANS molecule. We found that the efficiency of energy transfer from Trp residues to ANS was associated with the ability of proteins to enhance the ANS fluorescence. At the same molar concentration of protein, BSA enhanced ANS fluorescence most among these proteins; its Trp fluorescence was drastically quenched by the addition of ANS. Fluorescence enhancement of ANS in PLA2-ANS complex increased upon addition of Ca2+ or change of the buffer to acidicpH, resulting in a higher efficiency of energy transfer from Trp residues to ANS. There was limited ANS fluorescence enhancement with ovalbumin, lysozyme, cobrotoxin, and N-acetyltryptophanamide and a less efficient quenching in Trp fluorescence. The capabilities of proteins for binding with ANS correlated with the decrease in their Trp fluorescence being quenching by ANS. However, the microenvironment surrounding Trp residues of proteins did not affect the energy transfer. Based on these results, the factors that affected the energy transfer from Trp residues to ANS are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01890462
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  • 6
    Electronic Resource
    Electronic Resource
    Functional involvement of Lys-6 in the enzymatic activity of phospholipase A2 fromBungarus multicinctus (Taiwan banded krait) snake venom (1994)
    Springer
    The protein journal 13 (1994), S. 641-648 
    Details
    ISSN: 1573-4943
    Keywords: Snake venom ; phospholipase A2 ; chemical modification of Lys-6
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Phospholipase A2 (PLA2) fromBungarus multicinctus snake venom was subjected to Lys modification with 4-chloro-3,5-dinitrobenzoate and trinitrobenzene sulfonic acid, and one major carboxydinitrophenylated (CDNP) PLA2 and two trinitrophenylated (TNP) derivatives (TNP-1 and TNP-2) were separated by high-performance liquid chromatography. The results of amino acid analysis and sequence determination revealed that CDNP-PLA2 and TNP-1 contained one modified Lys residue at position 6, and both Lys-6 and Lys-62 were modified in TNP-2. It seemed that the Lys-6 was more accessible to modified reagents than other Lys residues in PLA2. Modification of Lys-6 caused a 94% drop in enzymatic activity as observed with CDNP-PLA2 and TNP-1. Alternatively, the enzyme modified on both Lys-6 and Lys-62 retained little PLA2 activity. Either carboxydinitrophenylation or trinitrophenylation did not significantly affect the secondary structure of the enzyme molecule as revealed by the CD spectra, and Ca2+ binding and antigenicity of Lys-6-modified PLA2 were unaffected. Conversion of nitro groups to amino groups resulted in a partial restoration of enzymatic activity of CDNP-PLA2 to 32% of that of PLA2. It reflected that the positively charged side chain of Lys-6 might play an exclusive role in PLA2 activity. The TNP derivatives could be regenerated with hydrazine hydrochloride. The biological activity of the regenerated PLA2 is almost the same as that of native PLA2. These results suggest that the intact Lys-6 is essential for the enzymatic activity of PLA2, and that incorporation of a bulky CDNP or TNP group on Lys-6 might give rise to a distortion of the interaction between substrate and the enzyme molecule, and the active conformation of PLA2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01890463
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  • 7
    Electronic Resource
    Electronic Resource
    Chemical modification of tryptophan residues in α-neurotoxins fromOphiophagus hannah (king cobra) venom (1995)
    Springer
    The protein journal 14 (1995), S. 89-94 
    Details
    ISSN: 1573-4943
    Keywords: King cobraα-neurotoxins ; tryptophan residues ; chemical modification ; nicotinic acetylcholine receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Twoα-neurotoxins, Oh-4 and Oh-7, from the king cobra (Ophiophagus hannah) venom were subjected to Trp modification with 2-nitrophenylsulfenyl chloride (NPS-Cl). One major NPS derivative was isolated from the modified mixtures of Oh-4 and two from Oh-7 by HPLC. Amino acid analysis and sequence determination revealed that Trp-27 in Oh-4, and Trp-30 and Trp-26 and 30 in the two Oh-7 derivatives, were modified, respectively. Sulfenylation of Trp-27 in Oh-4 caused about 70% drop in lethal toxicity and nicotinic acetylcholine receptor-binding activity. Modification of Trp-30 in Oh-7 resulted in the decrease of lethal toxicity by 36% and binding activity by 61%. The activities were further lost when the conserved Trp-26 in Oh-7 was modified. Sulfenylation of the Trp residues did not significantly affect the secondary structure of the toxins as revealed by the CD spectra. These results indicate that the Trp residues in these two longα-neurotoxins may be involved in the receptor binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888366
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  • 8
    Electronic Resource
    Electronic Resource
    Purification and characterization of a novel phospholipase A2 from king cobra (Ophiophagus hannah) venom (1995)
    Springer
    The protein journal 14 (1995), S. 451-456 
    Details
    ISSN: 1573-4943
    Keywords: King cobra phospholipase A2 ; histidine modification ; tryptophan modification ; fluorescence quenching
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A novel phospholipase A2, designated as Oh-DE-2, was isolated from the venom ofOphiophagus hannah (king cobra) by successive chromatography on SP-Sephadex C-25, DE-52, and Q-Sepharose columns. Oh-DE-2 with pI 5.1 showed an apparent molecular weight of 14 kD as revealed by SDS-PAGE and gel filtration. The amino acid sequence was homologous with those of PLA2s from Elapidae venoms. Oh-DE-2 was effectively inactivated byp-bromophenacyl bromide, indicating that the conserved His-48 is essential for its enzymatic activity. However, modification of the conserved Trp-19 did not cause a precipitous drop in the enzymatic activity of Oh-DE-2 as observed with PLA2s fromNaja naja atra andBungarus multicinctus venoms. A quenching study showed that the microenvironment of Trp in Oh-DE-2 was inaccessible to acrylamide, iodide, or cesium, a finding which was different from those observed with PLA2s fromN. naja atra andB. multicinctus venoms. These results might suggest that, unlike other PLA2 enzymes, Trp-19 in Oh-DE-2 is not directly involved in its enzymatic mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01888139
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  • 9
    Electronic Resource
    Electronic Resource
    The essentiality of His-47 and the N-terminal region for the binding of 8-anilinonaphthalene-1-sulfonate with Taiwan cobra phospholipase A2 (1996)
    Springer
    The protein journal 15 (1996), S. 255-260 
    Details
    ISSN: 1573-4943
    Keywords: Phospholipase A2 ; 8-anilinonaphthalene sulfonate ; pH-dependent fluorescence enhancement ; pH depencence of dissociation constant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The binding of the apolar fluorescent dye 8-anilinonaphthalene-1-sulfonate (ANS) toNaja naja atra phospholipase A2 (PLA2) as well as the enhancement of ANS fluorescence of the PLA2-ANS complex decreased with increasing pH in a pH range from 3 to 9. These pH-dependent curves can be well interpreted as the perturbation of an ionizable group with pK value of 5.8, which was assigned as His-47 in the active site of PLA2. The ionizable group with pK 5.8 was no longer observed after methylation of His-47, supporting the idea that thepH dependence of ANS binding arose from an electrostatic interaction between His-47 and the bound ANS. Removal of the N-terminal octapeptide of PLA2 caused a precipitous drop in the capability of PLA2 for binding with ANS and enhancing ANS fluorescence, reflecting that the integrity of the N-terminal region was essential for maintaining the hydrophobic character of the ANS-binding site. However, the nonpolarity of the ANS-binding site in the N-terminus-removed derivative was still partially retained at lowpH, but was completely lost at highpH. Evidently, the N-terminal region plays a more crucial role in ANS binding at highpH than at lowpH. These results indicate that hydrophobic interaction as well as electrostatic interaction are involved in the binding of ANS to PLA2, and that the relative contributions of both interactions in ANS fluorescence enhancement may be different under differentpH.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01887113
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  • 10
    Electronic Resource
    Electronic Resource
    Chemical modification of cationic residues in toxin a from king cobra (Ophiophagus hannah) venom (1996)
    Springer
    The protein journal 15 (1996), S. 95-101 
    Details
    ISSN: 1573-4943
    Keywords: Cationic residues ; chemical modification ; nicotinic acetylcholine receptor ; Toxin a
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The cationic groups of arginine and lysine residues inα-neurotoxin, Toxin a, isolated from king cobra (Ophiophagus hannah) venom were subjected to modification with trinitrobenzene sulfonate (TNBS) andp-hydroxyphenylglyoxal (HPG), respectively. The trinitrophenylated (TNP) derivatives of Toxin a at Lys-10, 56, or 71 showed approximately 25% residual lethality, and modifications on Lys-10 and 56 or Lys-10 and 50 resulted in a decrease of lethality by 84% and 86%, respectively. Modifications on Arg-34, 37, and 70 and Arg-34, 37, and 72 in Toxin a caused a decrease in lethality by 92% and 93%, respectively, and it almost completely lost its lethality and binding activity to nicotinic acetylcholine receptor (nAChR) when all four arginine residues were modified. These results indicate that in addition to the cationic residues on loop II (Arg-34, 37), loop III (Lys-50, 56), and the C-terminal tail (Arg-70, 72; Lys-71), Lys-10 on loop I is also related to the neurotoxicity of Toxin a.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01886815
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