Trypsin activation of porcine procolipase. Kinetics of activation and effects on lipid binding

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Abstract

The kinetics of trypsin activation of pancreatic procolipase was investigated and the pH dependence of the binding of procolipase and colipase to a tributyrine-bile salt interface studied. The Km was 0.06 mM and Kcat 8 s-1, and was of the same order of magnitude as for the activation of pancreatic zymogens. At basic pH values colipase had a higher affinity for the tributyrine-bile salt interface as compared to procolipase. The trypsin activation of procolipase ensures a rapid degradation of dietary lipids in the intestine.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Läkemedelskemi

Nyckelord

Originalspråkengelska
Sidor (från-till)63-66
Antal sidor4
TidskriftFEBS Letters
Volym185
Utgåva nummer1
StatusPublished - 1985 jun 3
PublikationskategoriForskning
Peer review utfördJa