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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
Stable URL: http://www.jstor.org/stable/8952
Page Count: 3
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Further Characterization of Brain Cholecystokinin-Converting Enzymes
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Abstract

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.

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