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  • 1
    Electronic Resource
    Electronic Resource
    Neurotoxins of Animal Venoms: Snakes (1973)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 42 (1973), S. 235-258 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bi.42.070173.001315
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Enzymatic and biological studies of cholera (Vibrio cholerae) toxin (1971)
    Springer
    Cellular and molecular life sciences 27 (1971), S. 858-859 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Untersuchung der Enterotoxine vonVibrio cholerae auf eine Reihe von Enzymaktivitäten und im Hinblick auf die Aufklärung des pathogenetischen Mechanismus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02136912
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  • 3
    Electronic Resource
    Electronic Resource
    The presence of al-leucyl-β-napthylamide hydrolyzing enzyme in snake venoms (1967)
    Springer
    Cellular and molecular life sciences 23 (1967), S. 439-440 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé Pour déterminer le caractère des exo-peptidases dans le venin des serpents on a employé comme substrat dul-leucyl-β-napthylamide. Des venins de 49 espèces et sous-espèces des 4 familles de serpents venimeux ont été étudiés. La capacité d'hydroliser ce substrat a été rencontrée assez souvent dans les venins des serpents venimeux quelles que joient leurs origines géographiques ou leurs différences génétiques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02142164
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Fine structural changes of myelinated nerve associated with copperhead envenomation (1972)
    Springer
    Acta neuropathologica 21 (1972), S. 68-75 
    Details
    ISSN: 1432-0533
    Keywords: Myelinated Nerve ; Venom ; Ultrastructure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The fine structure of right sciatic nerves of Swiss white mice was studied after being exposed to a venom solution ofAgkistrodon contortrix laticinctus (broad-banded copperhead) and to 0.9% NaCl solutions for periods of 1, 2 or 3 h. There was some “Wallerian-like” degeneration in all groups of nerves in the experiment. Additional neuropathological changes were noted in the nerves exposed to venom solutions. The connective tissue was affected most severely, while the basal lamina was unaffected. Schwann cells were vacuolated, and in the most extreme case, a type of myelin splitting occurred which was considered as a “demyelinative” effect. The results were compared to those of Martin and Rosenberg (1968) [15] on studies of the giant squid axon. References to additional fine structural studies of various other neuropathies were given.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688001
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  • 5
    Electronic Resource
    Electronic Resource
    Peroxidative activity of hemepeptides from horse heart cytochromec (1968)
    Springer
    Cellular and molecular life sciences 24 (1968), S. 219-221 
    Details
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Résumé L'hémoundécapeptide (HUP) a été préparé par digestion pepsique du cytochromec qui a été extrait et purifié à partir du cœur de cheval. L'hémooctapeptide (HOP) a été obtenu par digestion trypsique de l'HUP. L'un et l'autre ont donné des produits homogènes par chromatographie sur colonne et sur papier, par électrophorèse sur papier à différents pH et par analyse des acides aminés. On a effectué une analyse spectrométrique de HUP et HOP et déterminé leur activité peroxydasique dans diverses conditions. Ces 2 composés n'ont pas montré d'activité catalasique.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02152778
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    CIDNP study of the aromatic side chain interactions in myotoxina (1994)
    Springer
    The protein journal 13 (1994), S. 333-337 
    Details
    ISSN: 1573-4943
    Keywords: Myotoxina ; CIDNP ; aromatic side-chain interaction ; NMR line broadening ; Ca2+ ATPase calcium pump blocker
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract CIDNP and COSY measurements were applied to study aromatic side chain interactions and conformations in myotoxina, aCrotalus venom toxin which acts as blocker of the Ca2+ influx in the sarcoplasmic reticulum calcium pump. New evidence for the existence of a hydrophobic aromatic cluster at the amino terminus was obtained. This cluster consists of Tyr1, His5, His10, and (possibly) F12. The CIDNP data clearly establish that the usual order of the tyrosine 2, 6 and 3, 5 proton signals of Tyr, is inverted, because of the large diamagnetic shielding effects of one ring on the other. The lines of the 2, 6 ring protons of Tyr1, and proton 4 in each of His5 and His10 are significantly broadened, an outcome of the side-chain hydrophobic interaction. The aromatic cluster could possibly present a hydrophobic sticky patch for binding of toxin by Ca2+ ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01901566
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  • 7
    Electronic Resource
    Electronic Resource
    Secondary structure of pig skin proteodermatan sulfate: A perspective from Raman spectroscopic studies in aqueous solution (1989)
    New York : Wiley-Blackwell
    Biopolymers 28 (1989), S. 1935-1938 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Raman spectroscopic studies of pig skin proteodermatan sulfate in H2O are indicative of a well defined secondary structure consisting of α-helical, β-turn, and possibly “random” structures. The above conclusion is surprisingly close to the secondary structure of the “core” protein of pig skin proteodermatan sulfate proposed in the previous paper (V. Renugopalakrishnan et al., Biopolymers 28, 1923-1933, 1989) from FT-IR and CD spectroscopic studies in aqueous solution.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.360281110
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    Paper (German National Licenses)
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