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  Medicinal spices and vegetables from Africa : therapeutic potential against metabolic, inflammatory, infectious and systemic diseases

  edited by Victor Kuete

  Contents:
  Part I. Diverse degenerative diseases in Africa
  1. Diseases in Africa : an overview
  2. Management of inflammatory and nociceptive disorders in Africa
  3. Burden and health policy of cancers in Africa
  5. Management of infectious diseases in Africa
  6. Overview of governmental support across Africa toward the development and growth of herbal medicine
  7. Preparation, standardization, and quality control of medicinal plants in Africa
  Part II. Therapeutic potential of African medicinal spices and vegetables
  8. Antimicrobial activities of African medicinal spices and vegetables
  9. Anti-inflammatory and anti-nociceptive activities of African medicinal spices and vegetables
  10. Anticancer activities of African medicinal spices and vegetables
  11. Antiemetic African medicinal spices and vegetables
  12. African Medicinal Spices and Vegetables and Their Potential in the Management of Metabolic Syndrome
  13. Other health benefits of African medicinal spices and vegetables
  Part III. Popular African medicinal spices and vegetables, and their health effects
  14. Allium cepa
  15. Allium sativum
  16. Canarium schweinfurthii
  17. Cinnamon species
  18. Cymbopogon citratus
  19. Curcuma longa
  20. Lactuca sativa
  21. Mangifera indica L. (Anacardiaceae)
  22. Moringa oleifera
  23. Myristica fragrans : a review
  24. Passiflora edulis
  25. Petroselinum crispum. a Review
  26. Sesamum indicum
  27. African Medicinal Spices of Genus Piper
  28. Thymus vulgaris
  29. Syzygium aromaticum
  Index.

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• Article

  Improved pepsin inhibitor derived from activation peptide 1-16 of porcine pepsinogen.

  Harish Kumar PM, Kassell B.

  Biochemistry. 1977 Aug 23;16(17):3846-9.

  The peptide Leu-Val-Lys-Val-Pro-Leu-Val-Arg-Lys-Lys-Ser-Leu-Arg-Gln-Asn-Leu, a known pepsin inhibitor, is derived from the first 16 amino acids of porcine pepsinogen. It was prepared from the activation mixture and was modified by guanidination of its three lysine residues to form homoarginine residues. The modified peptide is a better pepsin inhibitor than the native peptide; for 50% inhibition of the milk clotting action of pepsin at pH 5.3, the molar ratio of peptide to pepsin required is 9 for the native inhibitor and only 2 for the guanidinated inhibitor. The dissociation constants (k1) of the inhibitor-pepsin complexes are 7 X 10(-8) and 1.4 X 10(-8) M for the native and guanidinated peptides, respectively. The guanidinated peptide is more resistant to digestion by pepsin at pH 3.5. The native and modified peptides partially protect pepsin from inactivation at pH 7. Stepwise removal of the amino-terminal Leu-Val-Har residues from the guanidinated inhibitor by Edman degradation decreases the pepsin-inhibiting activity only slightly at the first step, but markedly at the second and third steps. Thus, all of the amino-terminal sequence except the leucine residue is necessary for full activity.

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  PubMed