Open Daily: 10am - 10pm | Alley door pickup 10am - 7pm 3038 Hennepin Ave Minneapolis, MN
612-822-4611

  • Open Daily: 10am - 10pm
    Alley-side Pickup: 10am - 7pm

    3038 Hennepin Ave Minneapolis, MN
    612-822-4611

Open Daily: 10am - 10pm | Alley-side Pickup: 10am - 7pm
3038 Hennepin Ave Minneapolis, MN
612-822-4611
Processing of vasopeptides by carboxypeptidases

Processing of vasopeptides by carboxypeptidases

Vieira Pereira, Hugo Juarez

Paperback

Chemistry

ISBN10: 6209007120
ISBN13: 9786209007125
Publisher: Our Knowledge Publishing
Published: Aug 21 2025
Pages: 92
Weight: 0.30
Height: 0.22 Width: 6.00 Depth: 9.00
Language: English
The mesenteric arterial bed (MAB) is capable of secreting some soluble proteases that accumulate in the perfusion fluid. Our laboratory has been dedicated to characterizing these enzymes, among them elastase-2, previously described as a solely digestive enzyme, and now also presented as the main enzyme forming Ang II in rat MAB perfusate. In addition to this endopeptidase, carboxypeptidase activities were detected in this perfusate using synthetic substrates and vasopeptides such as ZVF, Ang I, and Bk. The des-Arg9-Bk-forming activity was recently characterized as CPB1. Once again, a protease previously described solely as digestive was found to process vasopeptides in rat LAM perfusate. Thus, the objective of this study was to determine the enzymes capable of acting on the C-terminal region of angiotensins, cleaving aromatic and aliphatic residues.

Also from

Vieira Pereira, Hugo Juarez

View All

Also in

Chemistry

View All