caa a22 4500 397558104 CHVBK 20180308164809.0 cr unu---uuuuu 161202e199610 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021470 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021470 Characterization of p92, Karyopherin β, Co-Purified with N-Acetylglucosamine-Bearing Nucleoporins from Rat Liver Nuclear Envelopes [Elektronische Daten] [Shigehito Makifuchi, Masaki Takeuchi, shigeru kawahire, Shoji Odani, Tohru Ichimura, Saburo Omata, Tsuneyoshi Horigome] A 92k protein (p92) was purified from the wheat germ agglutinin-Sepharose (WGA-Sepharose) bound fraction of a rat liver nuclear envelope salt-extract by DEAE-5PW and hydroxyapatite HPLCs. Partial amino acid sequence analysis of p92 revealed that it is karyopherin β, which was found recently in the cytosolic fraction. It was shown using anti-p92 antiserum that the protein is present in the nuclear envelope and cytosolic fractions, in almost the same amounts, but not in other subcellular fractions of rat liver. p92 bound to N-acetylglucosamine-bearing nucleoporins (GNPs) on WGA-Sepharose, but not directly to WGA. The amount of p92 found in the rat liver nuclear envelope fraction corresponded to about 10% of the nuclear pore complex in mass, and to as much as 140 mol of p92 per mol of nuclear pore complex. Hydrodynamic analysis of the purified p92 suggested that the molecule is present as a monomer and that it is a rod-shaped molecule. The interaction of p92 and GNPs seemed to be hydrophobic and ionic. Based on these results, the participation of nuclear envelope p92 in protein nuclear transport is discussed. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence importin β nationallicence karyopherin β nationallicence NLS receptor nationallicence nuclear transport nationallicence PTAC97 nationallicence Makifuchi Shigehito Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut Takeuchi Masaki Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut kawahire shigeru Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut Odani Shoji Department of Biology, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut Ichimura Tohru Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut Omata Saburo Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut Horigome Tsuneyoshi Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut The Journal of Biochemistry Oxford University Press 120/4(1996-10), 716-724 0021-924X 120:4<716 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021470 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021470 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Makifuchi Shigehito Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 700 1- Takeuchi Masaki Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 700 1- kawahire shigeru Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 700 1- Odani Shoji Department of Biology, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 700 1- Ichimura Tohru Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 700 1- Omata Saburo Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 700 1- Horigome Tsuneyoshi Department of Biochemistry, Faculty of Science, Niigata University 2-Igarashi, Niigata 950-21 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/4(1996-10), 716-724 0021-924X 120:4<716 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford