dipeptidyl aminopeptidase IV

dipeptidyl aminopeptidase IV

a digestive enzyme of the small intestine enterocytes (brush border).
References in periodicals archive ?
Enzymatic properties of dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis and its participation in virulence.
Molecular mechanism for connective tissue destruction by dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis.
Of cytoplasmic proteases, activites of alanyl aminopeptidase (84 nmol/h/mg protein) and dipeptidyl aminopeptidase IV (29 nmol/h/mg protein) were highest in the gut followed by head (68 and 23 nmol/h/mg protein, respectively) than all other body compartments of P.
Thus the head contained highest concentrations of arginyl aminopeptidase, leucyl aminopeptidase, tripeptidyl aminopeptidase, proline endopeptidase, and cathepsin D, while the gut contained highest levels of all lysosomal proteases tested in this study (except cathepsin D, which was highest in the thorax part) as well as alanyl aminopeptidase and dipeptidyl aminopeptidase IV out of cytoplasmic proteases.
Thus alanyl aminopeptidase was increased by 53%, arginyl aminopeptidase by 73%, leucyl aminopeptidase by 16%, dipeptidyl aminopeptidase IV by 17%, tripeptidyl aminopeptidase by 148% and proline endopeptidase by 111%.