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Structure-Function Relationships in the Interaction of Amphipathic Helical Polypeptides with the Gastric H/K ATPase

✍ Scribed by J. CUPPOLETTI; B. V. CHERNYAK; P. HUANG; D. H. MALINOWSKA

Book ID
119867928
Publisher
John Wiley and Sons
Year
1992
Tongue
English
Weight
194 KB
Volume
671
Category
Article
ISSN
0890-6564

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Interaction of polypeptides with the gastric (H++ K+)ATPase: melittin, synthetic analogs, and a potential intracellular regulatory protein
✍ John Cuppoletti; Danuta H. Malinowska πŸ“‚ Article πŸ“… 1992 πŸ› Springer 🌐 English βš– 525 KB

The 26 amino acid bee venom toxin, melittin, is an amphipathic helical polypeptide which inhibits the gastric (H+ + K+)ATPase. The site of interaction with the (H+ + K+)ATPase was shown to be the alpha subunit of the (H+ + K+)ATPase in studies using [125I]azidosalicylyl melittin, a radioactive photo