Dipeptidyl Peptidase IV from Human Serum: Purification, Characterization, and N-Terminal Amino Acid Sequence
| Autor: | Yasuhiro Watanabe, Yukio Fujimoto, Sachiko Iwaki-Egawa, Yasuoki Kikuya |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Adenosine Deaminase
Dipeptidyl Peptidase 4 Molecular Sequence Data Kidney Biochemistry Dipeptidyl peptidase Amidohydrolases Serine Adenosine deaminase Humans Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Amino Acid Sequence Molecular Biology Peptide sequence Dipeptidyl peptidase-4 chemistry.chemical_classification Sequence Homology Amino Acid biology Chemistry General Medicine Amino acid Transmembrane domain Enzyme biology.protein Sequence Analysis |
| Zdroj: | Journal of Biochemistry. 124:428-433 |
| ISSN: | 0021-924X |
| DOI: | 10.1093/oxfordjournals.jbchem.a022130 |
| Popis: | Dipeptidyl peptidase IV (DPP IV) in normal human serum was purified 14,400-fold with a 25% yield to homogeneity. The molecular weight of the purified enzyme was approximately 110,000 on SDS-PAGE, almost the same as that of human kidney membrane-bound DPP IV. No difference was found between the two enzymes enzymologically and immunologically, either in substrate specificity, susceptibility to inhibitors, or cross-reactivity with an anti-rat kidney DPP IV antibody, or in their ability to bind adenosine deaminase. However, the N-terminal amino acid sequence of serum DPP IV lacked the transmembrane domain of the membrane-bound enzyme and started at the 39th position, serine, from the N-terminus predicted from the cDNA nucleotide sequence. These results suggest that membrane-bound DPP IV loses its transmembrane domain upon release into the serum, and that its structure on the plasma membrane is not required for its binding to adenosine deaminase. |
| Databáze: | OpenAIRE |
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