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aminopeptidase

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a·mi·no·pep·ti·dase (-mn-ppt-ds, -dz, m-n-)
n.
Any of various enzymes that catalyze the hydrolysis of the terminal peptide bond at the amino end of a polypeptide.

aminopeptidase
an enzyme produced by the intestinal mucosa which completes the process of protein digestion by hydrolyzing the amino-terminal amino acids of peptides and some proteins, after the initial breakdown of protein to peptides has already taken place, e.g. the enzyme that removes the methionine coded by the initiation codon AUG.

aminopeptidase
Any of the hydrolases–enzymes, which catalyze the removal of amino terminal amino acids or dipeptides from a protein or peptide


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difficile was preliminarily identified with L-proline aminopeptidase activity (Pro Disc; Remel, Lenexa, KS, USA) but confirmed by PCR detection of the triose phosphate isomerase gene (7).
Others discuss the molecular and physiological aspects of the angiotensin IV-ondulain regulated aminopeptidase interaction, its regulatory effects on cellular function, its biochemical and physiological actions and role in the treatment of cardiovascular diseases, its effects in renal fibrogenesis, the role of vitamin D in the modulation of the pancreatic rennin-angiotensin system, and pharmacotherapeutic effects of angiotensin II type 1 receptor blockers.
ABSTRACT Leucine aminopeptidase (LAP) belongs to a family of ubiquitous peptidases, with roles in growth and development, stress responses and adaptation to changing environmental conditions.
 
 
 
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