Molecular heterogeneity of ferredoxin-NADP+ reductase from spinach leaves |
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Authors: | H Hasumi E Nagata S Nakamura |
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Affiliation: | 1. Department of Neuroscience Johns Hopkins University School of Medicine 725 North Wolfe Street Baltimore, Maryland 21205 USA;2. Department of Physiology Johns Hopkins University School of Medicine 725 North Wolfe Street Baltimore, Maryland 21205 USA |
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Abstract: | Highly purified ferredoxin-NADP+ reductase from spinach leaves showed at least eight different protein bands in the electrofocused gel. All of them were catalytically active and were adsorbed on a ferredoxin-Sepharose 4B affinity column. The N-terminal amino acid sequence of the main component species was analyzed by the automatic Edman degradation method. It was found that when the reductase was stored at 4 degrees C, new protein bands appeared in isoelectric focusing and sodium dodecyl sulfate polyacrylamide gel electrophoreses, but the appearance of the bands was suppressed by the addition of a protease inhibitor, diisopropyl fluorophosphate. This indicates that the molecular heterogeneity of the reductase may result from the digestion with a protease present in spinach leaves. |
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Keywords: | mAChR muscarinic acetylcholine receptor QNB quinuclidinyl benzilate PBS physiologic buffer solution Gpp(NH)p 5′guanylimidodiphosphate GN guanine nucleotides maximal binding capacity |
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