Purification and characterization of a biliverdin-associated protein from the hemolymph of Manduca sexta

التفاصيل البيبلوغرافية
العنوان: Purification and characterization of a biliverdin-associated protein from the hemolymph of Manduca sexta
المؤلفون: Jeffrey T. Trost, Bruce R. Adams, Walter G. Goodman
المصدر: Biochemistry. 24(5)
سنة النشر: 1985
مصطلحات موضوعية: medicine.medical_specialty, animal structures, Magnetic Resonance Spectroscopy, Invertebrate Hormones, Macromolecular Substances, Protein subunit, Biology, Moths, Biliverdin IX, Biochemistry, chemistry.chemical_compound, Internal medicine, Hemolymph, polycyclic compounds, medicine, Animals, Amino Acids, Bilin, Biliverdin, Binding protein, fungi, Biliverdine, biology.organism_classification, Chromatography, Ion Exchange, Proton magnetic resonance, Lepidoptera, Molecular Weight, Endocrinology, chemistry, Manduca sexta, Chromatography, Gel, Insect Proteins, Electrophoresis, Polyacrylamide Gel, Carrier Proteins, Crystallization
الوصف: A biliverdin binding protein, insecticyanin, has been isolated from the hemolymph of the fourth instar tobacco hornworm Manduca sexta. The protein has been purified to apparent homogeneity by conventional chromatography with a cumulative yield of 40-50%. The protein (Mw 71 600) is composed of three subunits (Mr 23 000). Each subunit binds one biliverdin molecule. Proton magnetic resonance spectroscopy and absorption spectroscopy demonstrate that the bilin is the biliverdin IX gamma isomer.
تدمد: 0006-2960
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34bcb0c2050c97809b27f071e55862fa
https://pubmed.ncbi.nlm.nih.gov/4096898
رقم الانضمام: edsair.doi.dedup.....34bcb0c2050c97809b27f071e55862fa
قاعدة البيانات: OpenAIRE