Biomaterial Database

Dipeptidyl peptidase IV from human serum: purification, characterization, and N-terminal amino acid sequence. 1998

S Iwaki-Egawa, and Y Watanabe, and Y Kikuya, and Y Fujimoto

Department of Clinical Biochemistry, Hokkaido College of Pharmacy, Otaru, Hokkaido, 047-0264, Japan. sachiko@hokuyakudai.ac.jp

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.

UI	MeSH Term	Description	Entries
D007668	Kidney	Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.	Kidneys
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000243	Adenosine Deaminase	An enzyme that catalyzes the hydrolysis of ADENOSINE to INOSINE with the elimination of AMMONIA.	Adenosine Aminohydrolase,Aminohydrolase, Adenosine,Deaminase, Adenosine
D000581	Amidohydrolases	Any member of the class of enzymes that catalyze the cleavage of amide bonds and result in the addition of water to the resulting molecules.	Amidases,Amidohydrolase
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D017386	Sequence Homology, Amino Acid	The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.	Homologous Sequences, Amino Acid,Amino Acid Sequence Homology,Homologs, Amino Acid Sequence,Homologs, Protein Sequence,Homology, Protein Sequence,Protein Sequence Homologs,Protein Sequence Homology,Sequence Homology, Protein,Homolog, Protein Sequence,Homologies, Protein Sequence,Protein Sequence Homolog,Protein Sequence Homologies,Sequence Homolog, Protein,Sequence Homologies, Protein,Sequence Homologs, Protein
D017421	Sequence Analysis	A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information.	Sequence Determination,Analysis, Sequence,Determination, Sequence,Determinations, Sequence,Sequence Determinations,Analyses, Sequence,Sequence Analyses
D043524	Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase	An amidohydrolase that removes intact asparagine-linked oligosaccharide chains from glycoproteins. It requires the presence of more than two amino-acid residues in the substrate for activity. This enzyme was previously listed as EC 3.2.2.18.	Glycopeptidase,Glycopeptidase A,Glycopeptidase F,Glycopeptide N-glycosidase,N-Glycanase,N-Glycosidase A,N-Glycosidase F,N-Oligosaccharide Glycopeptidase,PNGase A,PNGase F,Peptide N-Glycanase,Peptide N-Glycosidase,Peptide N-glycohydrolase F,Peptide-N(4)-(acetyl-beta-glucosaminyl)Asparagine Amidase,Peptide-N-Glycanase,Glycopeptidase, N-Oligosaccharide,Glycopeptide N glycosidase,N Glycanase,N Glycosidase A,N Glycosidase F,N Oligosaccharide Glycopeptidase,N-Glycanase, Peptide,N-Glycosidase, Peptide,N-glycohydrolase F, Peptide,N-glycosidase, Glycopeptide,Peptide N Glycanase,Peptide N Glycosidase,Peptide N glycohydrolase F
D018819	Dipeptidyl Peptidase 4	A serine protease that catalyses the release of an N-terminal dipeptide. Several biologically-active peptides have been identified as dipeptidyl peptidase 4 substrates including INCRETINS; NEUROPEPTIDES; and CHEMOKINES. The protein is also found bound to ADENOSINE DEAMINASE on the T-CELL surface and is believed to play a role in T-cell activation.	Antigens, CD26,CD26 Antigens,Dipeptidyl-Peptidase IV,Adenosine Deaminase Complexing Protein 2,CD26 Antigen,Antigen, CD26,Dipeptidyl Peptidase IV