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Subcellular Localization and Isoenzyme Pattern of Peroxidase and Polyphenol Oxidase in Beet Root (Beta vulgaris L.)
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
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4‐Methoxy‐α‐naphthol as a specific substrate for kinetic, zymographic and cytochemical studies on plant peroxidase activities
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Peroxidase isoenzymes in normal and habituated calli of sugar beet during transfer from light to darkness
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Subcellular localization and polymorphism of peroxidase in horse-radish tumour and teratoma tissue
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Disk Electrophoresis of Basic Proteins and Peptides on Polyacrylamide Gels
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Polyribonucleotide-directed Protein Synthesis using an E. coli Cell-free System
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Identification of Tyrosinase in Mushrooms by Isoelectric Focusing
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The vacuolar localization of a basic peroxidase isoenzyme responsible for the synthesis of α‐31,41‐anhydrovinblastine in Catharanthus roseus (L.) G. Don Leaves
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Synthese und Strukturuntersuchungen von Iodocupraten(I) X. [Co(cp)2]2[CuI3] und [Co(cp)2][Cu2I3] = 1/9{[Co(C(cp)2]9[Cu6I11]∞ 2[(Cu6I8)2]} [1] / Syntheses and Structure Analyses of Iodocuprates(I) X. [Co(cp)2]2[CuI3] and [Co(cp)2][Cu2I3] = 1/9{[Co(cp)2]9[Cu6I11]∞ 2[(Cu6I8)2]} [1]
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Incoming claims: where this work appears in other papers’ reference lists and arguments.
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