Results 191 to 200 of about 27,424 (235)
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Biochimica Et Biophysica Acta - General Subjects, 1983
The regional, cellular and subcellular distribution patterns of aminopeptidase N and dipeptidyl aminopeptidase IV were examined in rat small intestine. Aminopeptidase N of brush border membrane had maximal activity in the upper and middle intestine, while dipeptidyl aminopeptidase IV had a more uniform distribution profile with relatively high activity
R H Erickson
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The regional, cellular and subcellular distribution patterns of aminopeptidase N and dipeptidyl aminopeptidase IV were examined in rat small intestine. Aminopeptidase N of brush border membrane had maximal activity in the upper and middle intestine, while dipeptidyl aminopeptidase IV had a more uniform distribution profile with relatively high activity
R H Erickson
exaly +3 more sources
Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA
FEBS Letters, 1988 The complete primary structure (967 amino acids) of an intestinal human aminopeptidase N (EC 3.4.11.2) was deduced from the sequence of a cDNA clone. Aminopeptidase N is anchored to the microvillar membrane via an uncleaved signal for membrane insertion.
Jørgen Olsen +2 more
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Aminopeptidase N during the ontogeny of the chick
Differentiation, 2006Little is known about the production and function of metallopeptidases in embryonic development. One such enzyme, aminopeptidase N (APN), is present in several epithelia, the brain and angiogenic vessels in adults. APN promotes vascular growth and endothelial cell proliferation in physiological and pathological models of angiogenesis.
Gabin, Sihn +6 more
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The Structure and Main Functions of Aminopeptidase N
Current Medicinal Chemistry, 2007Aminopeptidase N (APN)/CD13 is a type II metalloprotease that belongs to the M1 family of the MA clan, which consists of 967 amino acids with a short N-terminal cytoplasmic domain, a single transmembrane part, and a large cellular ectodomain containing the active site. APN has a molecular weight of 110,000.
Yepeng, Luan, Wenfang, Xu
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Differential Inhibition of Aminopeptidase A and Aminopeptidase N by New .beta.-Amino Thiols
Journal of Medicinal Chemistry, 1994Aminopeptidase A (APA) is a highly selective peptidase, which cleaves the N-terminal Glu or Asp residues of biologically active peptides, and has therefore been proposed to be involved in angiotensin II and CCK8 metabolism. Highly potent and selective APA inhibitors are consequently required to study the physiological regulation of these two peptides ...
Chauvel, Eric +5 more
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Structure and Expression of Aminopeptidase N
1997Aminopeptidase N (APN) is a very abundant membrane protein in the microvillar membrane of the small intestinal absorptive epithelial cell the enterocyte 1, 2. APN is an ectopeptidase and from its position in the brush border membrane it faces the small intestinal lumen.
Kokholm, K +3 more
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Biological Chemistry Hoppe-Seyler, 1995
In addition to cystine aminopeptidase (oxytocinase) alanine aminopeptidase is present at high levels in the serum of pregnant women. In this study we compared the enzyme with membrane-bound aminopeptidase N purified from human placenta. Comparison of catalytic and immunological properties and N-terminal sequence analyses revealed that the enzymes were ...
Y, Watanabe +3 more
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In addition to cystine aminopeptidase (oxytocinase) alanine aminopeptidase is present at high levels in the serum of pregnant women. In this study we compared the enzyme with membrane-bound aminopeptidase N purified from human placenta. Comparison of catalytic and immunological properties and N-terminal sequence analyses revealed that the enzymes were ...
Y, Watanabe +3 more
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Betulinic Acid Inhibits Aminopeptidase N Activity
Planta Medica, 1998The triterpene betulinic acid inhibits the activity of aminopeptidase N (EC 3.4.11.2) in a dose-dependent manner. An IC50 of 7.3 +/- 1.4 microM was determined for betulinic acid. This inhibitory activity is higher than that of bestatin' (IC50 = 16.9 +/- 4.1 microM), a well known inhibitor of this enzyme.
M F, Melzig, H, Bormann
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An aminopeptidase N deficiency in dog small intestine
Research in Veterinary Science, 1997This study has identified a naturally occurring, specific deficiency of a brush border aminopeptidase N (ApN) in the small intestines of five clinically healthy dogs. ApN activity in mucosal homogenates of dog small intestine was reduced significantly in deficient animals (13.4 (1.1) nmol min-1 mg-1 protein, n = 5, P < 0.002) compared to healthy ...
P W, Pemberton +3 more
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