The CP-I Subunit of Adenosine Deaminase Complexing Protein from Calf Kidney Is Identical to Human, Mouse, and Rat Dipeptidyl Peptidase IV

Itzhak Ben-Shooshan, Abraham H. Parola

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The CP-I subunit of calf kidney adenosine deaminase complexing protein (ADCP), isolated by affinity chromatography based on Sepharose-4B immobilized adenosine deaminase, is identical with dipeptidyl peptidase IV. This finding is based on the following results: (a) Its M(r) = 110 kD, as determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis; (b) its catalytic activity toward Gly-Pro-p-nitroanilide; (c) its inhibition by serine protease inhibitor; and (d) by two peptide sequences resulting from its trypsin proteolysis. Accordingly, the CP-I subunit of ADCP isolated from bovine kidney is DPPIV (CD26). Thus, as anticipated, the high affinity between ADA subunits prevails even when they originate in different species. Copyright (C) 1998 Elsevier Science Inc. All rights reserved.

Original languageEnglish
Pages (from-to)289-292
Number of pages4
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume119
Issue number2
DOIs
StatePublished - 1 Jan 1998

Keywords

  • Affinity chromatography
  • Amino-acid sequence analysis
  • CD26
  • Gly-Pro-p-nitroanilide
  • Kinetic parameters
  • Malignancy marker
  • Serine protease inhibitors
  • Severe combined immunodeficiency (SCID)

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Molecular Biology

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