These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Purification and substrate specificity of an angiotensin converting elastase-2 from the rat mesenteric arterial bed perfusate.
    Author: Paula CA, Sousa MV, Salgado MC, Oliveira EB.
    Journal: Biochim Biophys Acta; 1998 Oct 14; 1388(1):227-38. PubMed ID: 9774738.
    Abstract:
    A soluble angiotensin (Ang) II-generating enzyme has been purified to homogeneity from the rat mesenteric arterial bed (MAB) perfusate by a combination of gel filtration and affinity chromatographies. The enzyme is a glycoprotein of 28.5 kDa (SDS-PAGE), whose N-terminal sequence is identical with that of the rat pancreatic elastase-2; therefore the enzyme will henceforth be referred to as rat MAB elastase-2. When Ang I was used as the substrate, the enzyme specifically released Ang II and the dipeptide His-Leu (Km=36 microM; Kcat=1530 min-1). The catalytic efficiency (Kcat/Km=42.5 min-1 microM-1) of this reaction was comparable to those of other known Ang I-converting enzymes. The proteolytic specificity of the purified enzyme toward mellitin, oxidized insulin B chain, somatostatin-14 and renin substrate tetradecapeptide suggested that the enzyme-substrate interaction was defined by an extended substrate binding site, typical of elastases-2 of pancreatic origin. According to the sensitivity of the rat MAB elastase-2 to various inhibitors this enzyme could be described as a member of the chymostatin-sensitive group of Ang II-forming serine proteases. The localization and biochemical properties of this enzyme suggest that it might play a role in the regional control of vascular tonus.
    [Abstract] [Full Text] [Related] [New Search]