| First Author | Ben-Shooshan I | Year | 1998 |
| Journal | Comp Biochem Physiol B Biochem Mol Biol | Volume | 119 |
| Issue | 2 | Pages | 289-92 |
| PubMed ID | 9629661 | Mgi Jnum | J:47827 |
| Mgi Id | MGI:1206141 | Doi | 10.1016/s0305-0491(97)00327-1 |
| Citation | Ben-Shooshan I, et al. (1998) The CP-I subunit of adenosine deaminase complexing protein from calf kidney is identical to human, mouse, and rat dipeptidyl peptidase IV. Comp Biochem Physiol B Biochem Mol Biol 119(2):289-92 |
| abstractText | 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. |
