Purification and properties of cytochrome b5 from the larval midgut of the southern armyworm (Spodoptera eridania) |
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| Affiliation: | 1. Institute of Applied Biology, Shanxi University, Taiyuan 030006, P.R.China;2. College of Life Science, Shanxi University, Taiyuan 030006, P.R.China;3. Modern Research Center for Traditional Chinese Medicine, Shanxi University, Taiyuan 030006, P.R.China;4. Institute of Plant Protection, Shanxi Academy of Agricultural Sciences, Taiyuan 030031, P.R.China;5. Department of Entomology, Kansas State University, Manhattan, KS 66506, USA;1. Department of Mathematics, Drexel University, United States of America;2. Department of Mathematics, Oregon State University, United States of America;3. Department of Mathematics, University of California, Riverside, United States of America |
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| Abstract: | The cytochrome b5-like protein in the microsomal fraction of southern armyworm (Spodoptera eridania) larval midguts was solubilized with bromelain and purified about 130-fold to a specific content of 55.4 nmoles per mg protein. The protein had protoheme as its prosthetic group, a molecular weight of 11,400 ± 600 and its amino acid content and spectral properties were similar to those of cytochrome b5 purified from rat liver microsomes by a similar procedure. The midpoint oxidation-reduction potential (E0′) was −57 mV. The results strongly suggest that the armyworm midgut cytochrome is a structurally similar protein to mammalian cytochrome b5. |
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