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Further Characterization of Brain Cholecystokinin-Converting Enzymes
Steven W. Ryder, Eugene Straus and Rosalyn S. Yalow
Proceedings of the National Academy of Sciences of the United States of America
Vol. 77, No. 6, [Part 2: Biological Sciences] (Jun., 1980), pp. 3669-3671
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/8952
Page Count: 3
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The brain cholecystokinin-converting enzymes that cleave intact cholecystokinin to its COOH-terminal dodecapeptide and octapeptide also cleave the synthetic dipeptides Arg-Ile (or Arg-Val or Arg-Leu) and Arg-Asp, respectively. Thus, they are not hormone-specific enzymes but are bond-specific. Ultracentrifuge studies demonstrate that there is Arg-Ile hydrolase activity associated with a protein greater in molecular weight than gamma globulin and that both Arg-Ile and Arg-Asp hydrolase activities are associated with one or more proteins between albumin and gamma globulin in molecular weight.
Proceedings of the National Academy of Sciences of the United States of America © 1980 National Academy of Sciences