Abstract
THERE is in blood a relatively high concentration of a specific trypsin inhibitor, the nature and identity of which are not fully established. In the presence of salts, it seems to form a stable stoichiometric addition complex with the enzyme, which is practically undissociated and enzymatically inactive1. Similar complexes also prevail between the enzyme and a score of other natural inhibitors, whereby, in the case of ovomucoid, complex formation can be largely prevented by chemical modification of trypsin2,3. Thus it was recently shown that the trypsin – ovomucoid complex has a dissociation constant K 1 = 5.8 × 10−9 M, whereas acetylated trypsin is inhibited to a much lesser degree, the dissociation constant being higher3 by a factor of about 102.
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References
Laskowski, M., and Laskowski, jun., M., “Adv. Prot. Chem.”, 9, 203 (1954).
Fraenkel-Conrat, H., Bean, R. S., and Lineweaver, H., J. Biol. Chem., 177, 385 (1949).
Sri Ram, J., Terminiello, L., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., 52, 451, 464 (1954).
Innerfield, I., Schwarz, A., and Angrist, A., J. Clin. Invest., 31, 1049 (1952).
Laufman, H., and Roach, H. D., A.M.A. Arch. Surgery, 66, 552 (1953).
Terminiello, L., Sri Ram, J., Bier, M., and Nord, F. F., Arch. Biochem. Biophys., [57, 252 (1955)].
Taylor, A., Overman, R. S., and Wright, I. S., J. Amer. Med. Assoc., 155, 347 (1954).
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BIER, M., SRI RAM, J. & NORD, F. Inhibition of Acyl Trypsins by Human Serum. Nature 176, 789–790 (1955). https://doi.org/10.1038/176789a0
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DOI: https://doi.org/10.1038/176789a0
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