Biological and Biochemical Characteristics of the Tetrapeptide Tuftsin, Thr-Lys-Pro-Arg

  • V. A. Najjar
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 121B)


The naturally occurring tetrapeptide tuftsin (Thr-Lsy-Pro-Arg) was discovered on the basis of its ability to stimulate the phagocytic activity of the blood neutrophil (25, 32, 33). It is active only in the free tetrapeptide form. However, originally the molecule is covalently bonded to its parent carrier molecule leukokinin. The latter is a leukophilic γ-globulin that binds specifically to the blood neutrophil. In fact, under appropriate conditions, utilizing low ionic strength isotonic solutions, one can readily isolate blood granulocytes that possess a coat of γ-globulin all of which chromatographs in only 1 of the 4 peaks of serum γ-globulin, peak IV on phosphocellulose columns (9, 10, 49). Furthermore, even in the presence of normal physiological solutions such as Krebs-Ringer one can recover from purified neutrophils the leukokinin fraction which stimulates phagocytosis. This occurs after release of its tuftsin peptide by a specific enzyme on the outer surface of the membrane (26).


Keyhole Limpet Hemocyanin Blood Neutrophil Leucine Aminopeptidase Elective Splenectomy Human Malignant Melanoma Antigen 
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Copyright information

© Plenum Press, New York 1980

Authors and Affiliations

  • V. A. Najjar
    • 1
  1. 1.Tufts University School of MedicineBostonUSA

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