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New methods of isolating bee venom peptides

✍ Scribed by Barbara E.C. Banks; Chris E. Dempsey; Frederick L. Pearce; Charles A. Vernon; Teresa E. Wholley


Book ID
102629589
Publisher
Elsevier Science
Year
1981
Tongue
English
Weight
470 KB
Volume
116
Category
Article
ISSN
0003-2697

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πŸ“œ SIMILAR VOLUMES


Spectroscopic investigations of peptide
✍ P. Walde; H. JΓ€ckle; P. L. Luisi; C. J. Dempsey; B. E. C. Banks πŸ“‚ Article πŸ“… 1981 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 691 KB

## Abstract The circular dichroism (CD) and ^1^H‐nmr properties of peptide 401, a bee venom component with 22 amino acid residues and two disulfide bridges, have been studied under a variety of conditions and compared with those of the structurally related octadecapeptide apamin. The major componen

Synthesis of the Mast Cell Degranulating
✍ Priv.-Doz. Dr. Christian Birr; Dr. Margot Wengert-MΓΌller πŸ“‚ Article πŸ“… 1979 πŸ› John Wiley and Sons 🌐 English βš– 272 KB πŸ‘ 2 views

**Potential value in the therapy of rheumatism and other inflammation processes** could attach to the MCD peptide from bee venom if it were available in larger quantities. The peptide consists of 22 amino acids and contains two disulfide bridges. Its first total synthesis has now been accomplished.

Structural aspects of the interaction of
✍ Roberto Strom; Franca Podo; Carlo Crifo; Carmen Berthet; Martin Zulauf; Giuseppe πŸ“‚ Article πŸ“… 1983 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 348 KB πŸ‘ 2 views

In aqueous solution, melittin structure, investigated by CD and 'H-nmr, depends on pH and ionic composition, which also regulate the aggregation state of the peptide. When interacting with phospholipids, however, melittin exhibits a right-handed helical conformation without any evidence of oligomeri