| Autor: |
Oliveira, Pedro L., Kawooya, John K., Ribeiro, José M.C., Meyer, Terrance, Poorman, Roger, Alves, Elias W., Walker, F. Ann, Machado, Ednildo A., Nussenzveig, Roberto H., Padovan, Gilberto J., Masuda, Hatisaburo |
| Zdroj: |
Journal of Biological Chemistry; May 1995, Vol. 270 Issue: 18 p10897-10901, 5p |
| Abstrakt: |
A heme-binding protein has been isolated and characterized from both the hemolymph and oocytes of the blood-sucking insect, Rhodnius prolixus. The protein from both sources is identical in most aspects studied. The Rhodniusheme-binding protein (RHBP) is composed of a single 15-kDa polypeptide chain coiled in a highly α-helical structure which binds non-covalently one heme/polypeptide chain. This RHBP is not produced by limited degradation of hemoglobin from the vertebrate host, since specific polyclonal antibodies against it do not cross-react with rabbit hemoglobin, and since it differs from hemoglobin in having a distinct amino-acid composition and NH2-terminal sequence. The spectrum of the dithionite-reduced protein has peaks at 426, 530, and 559 nm and resembles that of a b-type cytochrome. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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