Results 131 to 140 of about 40,140 (225)

Biliary aminopeptidase-N and the cholesterol crystallisation defect in cholelithiasis

open access: yes, 1995
Several biliary proteins have cholesterol crystallisation promoting activity. One of these glycoproteins is aminopeptidase-N, a canalicular ectoenzyme. This study attempted to localise aminopeptidase-N along the biliary tree, to assess its concentration ...
Mingrone, Geltrude
core  

Isolation and characterization of Schizosaccharomyces pombe mutants lacking aminopeptidase activity

open access: yes, 1991
A mutant strain of the fission yeast Schizosaccharomyces pombe defective in aminopeptidase I was isolated by screening for lack of activity against the chromogenic substrate lysine-β-naphthlamide in isolated colonies.
Arbesú, María José   +2 more
core   +1 more source

Inhibition of aminopeptidase N by two synthetic tripeptides

open access: yes, 1996
MR-387A1 (AHPA-Val-Pro) and A2 (AHPA-Val-Hyp) were prepared as aminopeptidase N inhibitors through the synthesis of peptide MR-387A and B analogues which contained 3-amino-2-hydroxy-4-phenyl butanoic acid (AHPA) as a zinc-chelating moiety.
Choong Hwan Lee   +5 more
core  

Safety evaluation of an extension of use of the food enzyme leucyl aminopeptidase from the genetically modified <i>Aspergillus oryzae</i> strain NZYM-BU. [PDF]

open access: yesEFSA J
EFSA Panel on Food Enzymes (FEZ)   +15 more
europepmc   +1 more source

Human aminopeptidase N is encoded by 20 exons

open access: yes, 1996
Aminopeptidase
Vogel, L K   +4 more
core  

Safety evaluation of a food enzyme containing oryzin and leucyl aminopeptidase activities and a heat-treated food enzyme containing only leucyl aminopeptidase activity from the non-genetically modified <i>Aspergillus</i> sp. strain FL 72-230. [PDF]

open access: yesEFSA J
EFSA Panel on Food Enzymes (FEZ)   +21 more
europepmc   +1 more source

Characterization of Aminopeptidase Activities in Arabidopsis Thaliana Seedlings

open access: yes, 2013
Aminopeptidases are exopeptidases that are responsible for the removal of an amino acid residue from the N-terminus of peptides and protein substrates.
Noble, Gerald   +3 more
core  

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