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Two isoforms of a protease inhibitor were isolated by ion-exchange chromatography of tepary bean (Phaseolus acutifolius G.) seed proteins. The main isoform was used to determine the amino acid sequence of the protein. It is an 80 amino acid residue protein with a molecular mass of 8765 Da, showing sequence homology with the Bowman-Birk family of protease inhibitors. Several regions with amino acid microheterogeneity were found, corroborating the possible presence of isoforms. Mass spectrometry analysis was carried out to confirm isoforms. The presence of dimer and trimer forms of the inhibitor was shown through electrophoresis and mass spectrometry. Another unusual characteristic for this inhibitor was its ability to bind metals. The presence of four sequential histidines at the N-terminal end of the protein could account for this binding. Mass spectrometry and atomic absorption spectroscopy support the presence of calcium in the native inhibitor.  相似文献
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Studies on the diurnal variations of nitrate reductase (NR) activity during the life cycle of synchronized Chlorella sorokiniana cells grown with a 7:5 light-dark cycle showed that the NADH:NR activity, as well as the NR partial activities NADH:cytochrome c reductase and reduced methyl viologen:NR, closely paralleled the appearance and disappearance of NR protein as shown by sodium dodecyl sulfate gel electrophoresis and immunoblots. Results of pulse-labeling experiments with [35S]methionine further confirmed that diurnal variations of the enzyme activities can be entirely accounted for by the concomitant synthesis and degradation of the NR protein.  相似文献
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Incubation of casein and water-soluble soybean protein, separately or together, at 10 mg/ml with horseradish peroxidase (2.4 or 24 M) and H2O2 (1.8 or 18 mM) at pH 9.0 (0.2 M borate buffer) for 24 hr at 37°C in air led to formation of higher molecular weight compounds as determined by sodium dodecyl sulfate polyacrylamide disc gel electrophoresis. Incubation under the same conditions with peroxidase alone (in air) gave a smaller amount of higher molecular weight compounds. Incubation of lysozyme separately or with water-soluble soybean protein did not produce detectable amounts of higher molecular weight compounds. These results are discussed in terms of previously observed di- and tertyrosine isolated from peroxidase/H2O2-treated and naturally occurring proteins following acid hydrolysis. Transglutaminase, lipoxygenase, polyphenol oxidase, and lysyl oxidase are examples of other enzymes that can cross link proteins.  相似文献
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