Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.

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Standard

Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. / Cowell, G M; Kønigshøfer, E; Danielsen, E M; Hansen, O C; Engberg, J; Hunziker, W; Olsen, Jørgen; Møller, Jette; Laustsen, Lotte; Welinder, K G.

I: FEBS Letters, Bind 238, Nr. 2, 1988, s. 307-14.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Cowell, GM, Kønigshøfer, E, Danielsen, EM, Hansen, OC, Engberg, J, Hunziker, W, Olsen, J, Møller, J, Laustsen, L & Welinder, KG 1988, 'Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.', FEBS Letters, bind 238, nr. 2, s. 307-14.

APA

Cowell, G. M., Kønigshøfer, E., Danielsen, E. M., Hansen, O. C., Engberg, J., Hunziker, W., Olsen, J., Møller, J., Laustsen, L., & Welinder, K. G. (1988). Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Letters, 238(2), 307-14.

Vancouver

Cowell GM, Kønigshøfer E, Danielsen EM, Hansen OC, Engberg J, Hunziker W o.a. Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. FEBS Letters. 1988;238(2):307-14.

Author

Cowell, G M ; Kønigshøfer, E ; Danielsen, E M ; Hansen, O C ; Engberg, J ; Hunziker, W ; Olsen, Jørgen ; Møller, Jette ; Laustsen, Lotte ; Welinder, K G. / Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA. I: FEBS Letters. 1988 ; Bind 238, Nr. 2. s. 307-14.

Bibtex

@article{e2bffe9099fa11dd86a6000ea68e967b,
title = "Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.",
abstract = "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. A domain constituting amino acid 250-555 positioned within the catalytic domain shows very clear homology to E. coli aminopeptidase N and contains Zn2+ ligands. Therefore these residues are part of the active site. However, no homology of the anchor/junctional peptide domain is found suggesting that the juxta- and intra-membraneous parts of the molecule have been added/preserved during development. It is speculated that this part carries the apical address.",
author = "Cowell, {G M} and E K{\o}nigsh{\o}fer and Danielsen, {E M} and Hansen, {O C} and J Engberg and W Hunziker and J{\o}rgen Olsen and Jette M{\o}ller and Lotte Laustsen and Welinder, {K G}",
note = "Keywords: Amino Acid Sequence; Aminopeptidases; Animals; Antigens, CD13; Base Sequence; Catalysis; Cloning, Molecular; Codon; DNA; Escherichia coli; Humans; Intestines; Molecular Sequence Data; Nucleic Acid Hybridization; Protein Biosynthesis; RNA, Messenger; Rabbits; Sequence Homology, Nucleic Acid; Swine",
year = "1988",
language = "English",
volume = "238",
pages = "307--14",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "2",

}

RIS

TY - JOUR

T1 - Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA.

AU - Cowell, G M

AU - Kønigshøfer, E

AU - Danielsen, E M

AU - Hansen, O C

AU - Engberg, J

AU - Hunziker, W

AU - Olsen, Jørgen

AU - Møller, Jette

AU - Laustsen, Lotte

AU - Welinder, K G

N1 - Keywords: Amino Acid Sequence; Aminopeptidases; Animals; Antigens, CD13; Base Sequence; Catalysis; Cloning, Molecular; Codon; DNA; Escherichia coli; Humans; Intestines; Molecular Sequence Data; Nucleic Acid Hybridization; Protein Biosynthesis; RNA, Messenger; Rabbits; Sequence Homology, Nucleic Acid; Swine

PY - 1988

Y1 - 1988

N2 - 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. A domain constituting amino acid 250-555 positioned within the catalytic domain shows very clear homology to E. coli aminopeptidase N and contains Zn2+ ligands. Therefore these residues are part of the active site. However, no homology of the anchor/junctional peptide domain is found suggesting that the juxta- and intra-membraneous parts of the molecule have been added/preserved during development. It is speculated that this part carries the apical address.

AB - 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. A domain constituting amino acid 250-555 positioned within the catalytic domain shows very clear homology to E. coli aminopeptidase N and contains Zn2+ ligands. Therefore these residues are part of the active site. However, no homology of the anchor/junctional peptide domain is found suggesting that the juxta- and intra-membraneous parts of the molecule have been added/preserved during development. It is speculated that this part carries the apical address.

M3 - Journal article

C2 - 2901990

VL - 238

SP - 307

EP - 314

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 2

ER -

ID: 6586586