Weitere Untersuchungen zur Aminosäuresequenz des Melittins, II: Bevorzugte Spaltung der Valin-, Leucin- und Isoleucinbindungen durch α-Protease aus Crotalus atrox-Gift

Weitere Untersuchungen zur Aminosäuresequenz des Melittins, II: Bevorzugte Spaltung der Valin-, Leucin- und Isoleucinbindungen durch α-Protease aus Crotalus atrox-Gift

Degradation of melittin with α-Protease from Crotalus atrox venom (rattlesnake) confirmed the amino acid sequence of the toxic main peptide from bee venom. Hydrolysis occured mainly at the peptide bonds whose amino groups were provided by hydrophobic side chains such as valine, leucine and isoleucin...

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Veröffentlicht in:Zeitschrift für Naturforschung. B, A journal of chemical sciences A journal of chemical sciences, 1969-04, Vol.24 (4), p.415-418
1. Verfasser: Jentsch, Joachim
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Sprache:eng
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container_title Zeitschrift für Naturforschung. B, A journal of chemical sciences
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creator Jentsch, Joachim
description Degradation of melittin with α-Protease from Crotalus atrox venom (rattlesnake) confirmed the amino acid sequence of the toxic main peptide from bee venom. Hydrolysis occured mainly at the peptide bonds whose amino groups were provided by hydrophobic side chains such as valine, leucine and isoleucine bonds. However, on the contrary one glutamine bond was cleaved. Neverthelness, regarding the relatively high specificity, rattlesnake venom protease may be a valuable reagent for further sequence studies.
doi_str_mv 10.1515/znb-1969-0409
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title Weitere Untersuchungen zur Aminosäuresequenz des Melittins, II: Bevorzugte Spaltung der Valin-, Leucin- und Isoleucinbindungen durch α-Protease aus Crotalus atrox-Gift
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