نتایج جستجو برای: Aminopeptidase N

تعداد نتایج: 978986  

Journal: :Cancer research 1993
A Menrad D Speicher J Wacker M Herlyn

A cell surface protein expressed on melanoma cells, but not on normal melanocytes, was biochemically and functionally characterized. Microsequencing of the M(r) 143,000 affinity-purified protein revealed amino acid sequence identity to aminopeptidase N (EC 3.4.11.2). In situ expression, indirect immunofluorescence, and Western blotting demonstrated that aminopeptidase N is tightly associated wi...

Journal: :Applied and environmental microbiology 1991
I J van Alen-Boerrigter R Baankreis W M de Vos

The chromosomal pepN gene encoding lysyl-aminopeptidase activity in Lactococcus lactis has been identified in a lambda EMBL3 library in Escherichia coli by using an immunological screening with antiserum against a purified aminopeptidase fraction. The pepN gene was localized and subcloned in E. coli on the basis of its expression and hybridization to a mixed-oligonucleotide probe for the previo...

Journal: :Gut 1995
L Núñez L Amigo G Mingrone A Rigotti L Puglielli A Raddatz F Pimentel A V Greco S González J Garrido

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 in a series of 98 patients subjected to abdominal surgery, 40 of them without gall stones, and to correlate its concentration with cholesterol ...

Journal: :Journal of the National Cancer Institute 2002
Yuji Mishima Yuko Matsumoto-Mishima Yasuhito Terui Misa Katsuyama Muneo Yamada Masaki Mori Yukihito Ishizaka Kazuma Ikeda Jun-ichiro Watanabe Nobuyuki Mizunuma Hirotoshi Hayasawa Kiyohiko Hatake

BACKGROUND Attachment of leukemic cells to vascular endothelial cells induces the vascular endothelial cells to release endothelial cell-derived interleukin 8 (endothelial IL-8), which then induces leukemic cells to undergo apoptosis. NB4, a human promyelocytic leukemic cell line that expresses high levels of cell-surface CD13/aminopeptidase N, does not undergo endothelial IL-8-induced apoptosi...

Journal: :American journal of respiratory and critical care medicine 2000
K Tani F Ogushi L Huang T Kawano H Tada N Hariguchi S Sone

CD13/aminopeptidase N (E.C.3.4.11.2) is an ectoenzyme located in the outer membrane of a variety of cells. Because aminopeptidase expression was shown to be upregulated by a Th1-related cytokine, IFN-gamma, we examined here the significance of CD13/aminopeptidase N in pulmonary sarcoidosis. The activity of aminopeptidase in bronchoalveolar lavage fluid (BALF) was significantly higher in patient...

Journal: :American journal of physiology. Renal physiology 2007
Adolfo Varona Lorena Blanco José I López Javier Gil Ekaitz Agirregoitia Jon Irazusta Gorka Larrinaga

Peptides play important roles in cell regulation and signaling in many tissues and are regulated by peptidases, most of which are highly expressed in the kidney. Several peptide convertases have a function in different tumor stages, and some have been clearly characterized as diagnostic and prognostic markers for solid tumors, including renal cancer; however, little is known about their in vivo...

Journal: :Infection and immunity 2003
Araceli Contreras-Rodriguez Bernardo Ramirez-Zavala Andrea Contreras Gerhardt G Schurig Nammalwar Sriranganathan Ahide Lopez-Merino

An immunogenic aminopeptidase was purified from Brucella melitensis strain VTRM1. The purification procedure consisted of ammonium sulfate fractionation and three chromatographic steps. This procedure resulted in a yield of 29% and a 144-fold increase in specific activity. The aminopeptidase appeared to be a monomeric enzyme with a molecular mass of 96 kDa and an isoelectric point of 4.8. Its a...

Journal: :Blood 1990
R A Ashmun A T Look

We previously found that the myeloid cell surface glycoprotein CD13 (gp150) is identical to aminopeptidase N (EC 3.4.11.2), a widely distributed membrane-bound, zinc-dependent metalloprotease with an extracellular enzymatic domain that cleaves N-terminal amino acid residues from oligopeptides (J Clin Invest 83:1299, 1989). As a first step toward defining the function of this molecule on myeloid...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید