Evidence for the enzymic degradation of thyrotropin-releasing-hormone (trh) and pseudo-hormone (pyroglutamyl-histidyl-amphetamine) by calf liver pyroglutamine-amino-peptidase

Add time:08/16/2019    Source:sciencedirect.com

1.1. TRH and acid TRH were submitted to pyroglutamate amino peptidase digestion in vitro. The resulting cyclized compound corresponding to diketopiperazines of His-Pro were identified on paper electrophoregrams.2.2. The pseudo-hormones: Pyroglutamyl-Histidyl-Amphetamine, Pyroglutamyl-Histidyl-prolyl-Amphetamine, Pyroglutamyl-Amphetamine, Pyroglutamyl-Histidyl-O-Me were submitted to pyroglutamate amino peptidase digestion and the enzymic digests revealed the presence of free amphetamine. The result indicated that pyroglutamate aminopeptidase not only released N-terminal pyroglutamic acid but continuously hydrolyzed, step-wise the next amino acid probably as a result of amino peptidase contamination of animal liver origin.3.3. The prolinamides, Prolyl-Amphetamine and Pyroglutamyl-Histidyl-Prolyl-Amphetamine, were found independently to resist prolinase digestion.

We also recommend Trading Suppliers and Manufacturers of pyroglutamyl-((N3)-imidazolylmethyl)-histidyl-n-amylprolinamide (cas 107810-09-3). Pls Click Website Link as below: cas 107810-09-3 suppliers

Prev:Cloning and characterization of a glycosyltransferase gene involved in the biosynthesis of anthracycline antibiotic β-rhodomycin from Streptomyces violaceus
Next:X-ray conformational analysis of the potent thyroliberin analogue l-pyroglutamyl-β-(2-thienyl)-l-alanyl-l-prolinamide☆)