Results 131 to 140 of about 6,277 (184)

Diploid chromosome-level genome assembly and annotation for Lycorma delicatula. [PDF]

open access: yesSci Data
Snead AA   +4 more
europepmc   +1 more source

Effect of ACE mutations on blood ACE phenotype parameters. [PDF]

open access: yesPLoS One
Kryukova OV   +9 more
europepmc   +1 more source

Nutritional value, antibacterial activity, ACE and DPP IV inhibitory of red pomegranate seeds protein and peptides. [PDF]

open access: yesSci Rep
Akbarbaglu Z   +5 more
europepmc   +1 more source

Bidirectional relation between dipeptidyl peptidase 4 and angiotensin II type I receptor signaling.

open access: yesAm J Physiol Cell Physiol
Martins FL   +3 more
europepmc   +1 more source

Determination of peptidyl dipeptidase activity in 24 bacterial species

open access: closedCanadian Journal of Microbiology, 1990
Of 24 bacterial species examined for lisinopril refractive peptidyl dipeptidase activity, only 8 contained activity. Activity in Pseudomonas maltophilia was more than fourfold higher than that of any other species. Pseudomonas maltophilia may be unique among bacteria in possessing high peptidyl dipeptidase activity that is both EDTA inhibitable and ...
Joanne Stevens   +2 more
openalex   +4 more sources

Peptidyl dipeptidase in rabbit brain microvessels

open access: closedBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
The activity of peptidyl dipeptidase (peptidyldipeptide hydrolase, EC 3.4.15.1), also known as angiotensin-converting enzyme, was studied in small blood vessel preparations isolated from rabbit brain. The vascular preparation contained arterioles and capillaries and was essentially free of extravascular material.
Peter Brecher   +3 more
openalex   +4 more sources

Detection of essential arginine in bacterial peptidyl dipeptidase-4: Arginine is not the anion binding site

open access: closedBiochemical and Biophysical Research Communications, 1989
Peptidyl dipeptidase-4 from Pseudomonas maltophilia was modified with the arginine reagents p-hydroxyphenylglyoxal and 2,3-butanedione. The enzyme was inactivated in a pseudo-first-order manner by p-hydroxyphenylglyoxal with a half-time of 72 min. Inactivation by 2,3-butanedione was biphasic with a rapid phase followed by a slower inactivation to less ...
Joseph J. Lanzillo   +2 more
openalex   +3 more sources

Peptidyl-dipeptidase A/angiotensin I-converting enzyme

open access: closed, 2004
Publisher Summary This chapter discusses the tissue distribution and the substrate specificity of peptidyl-dipeptidase A/angiotensin I-converting enzyme. Angiotensin I-Converting Enzyme (ACE) is a zinc metallopeptidase that belongs to the gluzincin family (clan MA) of metalloproteases of which thermolysin is the prototype.
Pierre Corvol   +2 more
openalex   +3 more sources

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