Hemocyanins in Spiders, XVIII. Complete amino-acid sequence of subunit e from Eurypelma californicum hemocyanin
| Autor: | Bernt Linzen, Hans-Jürgen Schneider, Gertraud Feldmaier, Agnes Henschen, Friedrich Lottspeich, Raimund Drexel |
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| Rok vydání: | 1983 |
| Předmět: |
Chemical Phenomena
Formates Protein subunit Proteolysis medicine.medical_treatment Lysine Biology Biochemistry chemistry.chemical_compound Endopeptidases medicine Animals Chymotrypsin Trypsin Amino Acid Sequence Cyanogen Bromide Peptide sequence medicine.diagnostic_test Hydrolysis Serine Endopeptidases Hemocyanin Spiders Anatomy Peptide Fragments Chemistry chemistry Hemocyanins biology.protein Cyanogen bromide medicine.drug |
| Zdroj: | Hoppe-Seyler's Zeitschrift fur physiologische Chemie. 364(10) |
| ISSN: | 0018-4888 |
| Popis: | The complete amino-acid sequence of subunit e of the hemocyanin from the tarantula, Eurypelma californicum, was determined by a combination of manual and automated methods. By limited proteolysis with chymotrypsin, two large fragments (e-CHn 29 and e-CHn 42) were obtained. The large peptides were further cleaved with cyanogen bromide, trypsin (with and without prior blocking of lysine residues), chymotrypsin, Staphylococcus aureus proteinase, Astacus fluviatilis proteinase, or 25% formic acid. The complete chain comprises 621 residues. A remarkable feature of the sequence is a hexapeptide -His-His-Trp-His-Trp-His- which is believed to take part in the binding of copper. |
| Databáze: | OpenAIRE |
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