Characterization of mouse carboxypeptidase N small active subunit gene structure.

N Small Active Subunit Gene Structure Characterization of Mouse Carboxypeptidase

Plasmin alters the activity and quaternary structure of human plasma carboxypeptidase N.

Human CPN (carboxypeptidase N) is a tetrameric plasma enzyme containing two glycosylated 83 kDa non-catalytic/regulatory subunits that carry and protect two active catalytic subunits. Because CPN can regulate the level of plasminogen binding to cell surface proteins, we investigated how plasmin cleaves CPN and the consequences. The products of hydrolysis were analysed by activity assays, Wester...

Targeted disruption of the gene encoding the murine small subunit of carboxypeptidase N (CPN1) causes susceptibility to C5a anaphylatoxin-mediated shock.

Carboxypeptidase N (CPN) is a plasma zinc metalloprotease, which consists of two enzymatically active small subunits (CPN1) and two large subunits (CPN2) that protect the protein from degradation. Historically, CPN has been implicated as a major regulator of inflammation by its enzymatic cleavage of functionally important arginine and lysine amino acids from potent phlogistic molecules, such as...

Overexpression of Mitochondrial Genes (Mitochondrial Transcription Factor A and Cytochrome c Oxidase Subunit 1) in Mouse Metaphase II Oocytes following Vitrification via Cryotop

Background: Gamete cryopreservation is an inseparable part of assisted reproductive technology, and vitrification is an effective approach to the cryopreservation of oocytes. The aim of this study was to investigate vitrification effects on the expression levels of mitochondrial transcription factor A (Tfam) and mitochondrial-encoded cytochrome c oxidase subunit 1 (Cox1) in mouse metaphase II o...

Dissociation of Bovine 6S Procarboxypeptidase A by Reversible Condensation with 2,3-Dimethyl Maleic Anhydride: Application to the Partial Characterization of Subunit III (subunit isolation/free carboxypeptidase A zymogen/inactive serine protease/inactivating deletion)

Bovine 6S procarboxypeptidase A can be dissociated into its three subunits by acylation with dimethyl maleic anhydride. The deacylated subunits are obtained in a largely native form due to instability of the bonds to dimethyl maleate at pH values near neutrality. The seven first residues of subunit III are identical to residues 18-24 of bovine chymotrypsinogen B and very similar with the same r...