Dipeptidyl peptidase IV from human serum: purification, characterization, and N-terminal amino acid sequence.
J Biochem
; 124(2): 428-33, 1998 Aug.
Article
em En
| MEDLINE
| ID: mdl-9685737
ABSTRACT
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.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Dipeptidil Peptidase 4
Limite:
Humans
Idioma:
En
Revista:
J Biochem
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
Japão