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Volume 37 (1993)
- Issue 6 Pages 341-
- Issue 5 Pages 255-
- Issue 4 Pages 203-
- Issue 3 Pages 141-
- Issue 2 Pages 55-
- Issue 1 Pages 3-
Volume 37, Issue 2
Displaying 1-9 of 9 articles from this issue
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1993 Volume 37 Issue 2 Pages 55-57
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
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1993 Volume 37 Issue 2 Pages 58-61
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
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1993 Volume 37 Issue 2 Pages 62-67
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
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1993 Volume 37 Issue 2 Pages 68-96
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
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1993 Volume 37 Issue 2 Pages 97-108
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
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Masahiro Hosono, Hiroaki Kawauchi, Kazuo Nitta, Yoshio Takayanagi, Hir ...1993 Volume 37 Issue 2 Pages 109-115
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSWe have examined the existence of lectin activity in saline-extracted fractions of fish roe. Cell agglutination was observed in 13 of 19 fish species (68%), especially in Cypriniformes and Salmoniformes. A rhamnose-binding lectin was isolated from Osmerus eperlanus mordax (Olive rainbow smelt, Osmeridae, Salmoniformes) roe by affinity chromatography and ion-exchange chromatography. This lectin, termed OML, agglutinated rabbit and human ABO blood group erythrocytes and sarcoma 180 murine tumor cells. OML-induced hemagglutination was inhibited by L-rhamnose and α-galactosyl oligosaccharides. The apparent molecular weight of OML was estimated to be 26kDa on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing condition. The N-terminal 29 amino acid sequence of OML was determined as follows; VTTDIXEGQQATLNXGSSVINVVSANYGR (X: not determined).View full abstractDownload PDF (1726K) -
Motoo Matsuda, Kazumasa Matsumoto, Yukiho Imai, Mika Kikuchi, Choji Ka ...1993 Volume 37 Issue 2 Pages 117-121
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSPulsed-field gel electrophoretic profiles of the respective, undigested and intact chromosomal DNAs, prepared from three species of thermophilic Campylobacter (C. coli, C. jejuni and C. lari) demonstrated that the chromosomal DNAs from C. coli JCM 2529T, four isolated strains of C. coli, C. jejuni JCM 2013 and four isolated strains of C. jejuni migrated to around 1, 900kb, and the chromosomal DNAs from C. lari JCM 2530T migrated to around 1, 640kb. Chromosomal DNAs from 15 isolated strains of C. lari also migrated to almost the same extent as the DNAs from the C. lari type strain to around 1, 640kb. This result clearly demonstrates that pulsed-field gel electrophoresis (PFGE) is useful for the discrimination of C. lari from two other thermophilic species of Campylobacter (C. coli and C. jejuni).
When the chromosomal DNAs prepared from the three Campylobacter species were digested with the restriction enzyme ApaI, electrophoretic profiles of the undigested chromosomal DNAs also demonstrated PFGE to be useful for that discrimination.View full abstractDownload PDF (3128K) -
Takashi Manabe, Shigeru Terabe1993 Volume 37 Issue 2 Pages 123-128
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe performance of capillary gel electrophoresis, employing untreated fused silica capillaries, was examined in the electrophoretic analysis of oligonucleotides. A buffer solution containing acrylamide was filled in the capillaries and then polymerization was initialized. The rate of polymerization was controlled by adjusting the concentration of ammonium persulfate not to form air bubbles in the capillaries. Acrylamide was polymerized both in the presence and in the absence of N, N-methylenebisacrylamide, a cross-linker. The gel capillaries were successfully used for the single base resolution of oligodeoxyadenylic acids (40-mer to 60-mer) and high resolution analysis of pBR 322 HaeIII digested fragments. These results showed that the polyacrylamide gel capillaries prepared in untreated silica capillaries are practically useful in the analysis of oligonucleotides and DNA fragments.View full abstractDownload PDF (650K) -
2 substrain derived from HeLa cellsIwao Koyama, Ricardo Makiya, Kazuyuki Hirano, Tsugikazu Komoda, Torgny ...1993 Volume 37 Issue 2 Pages 129-136
Published: April 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSWe purified an alkaline phosphatase (AP) from Hep. 2 substrain derived from HeLa cells, by immunoaffinity chromatography using the combination of anti-placental and anti-intestinal enzyme antibodies. The cell extract was applied to a column coupled with anti-intestinal AP monoclonal antibody. The enzyme was eluted, dialyzed and then applied to a column linked to anti-placental AP monoclonal antibody. Although the purified enzyme showed a single catalytically active band on conventional polyacrylamide gel electrophoresis, it was separated into two bands on SDS-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence up to 17th residue that the AP was an intermediate form of the placental and intestinal isozyme. The treatment of the Hep. 2 cell with phosphatidylinositol-specific phospholipase C stoichiometrically released the two different subunits of AP. These results clearly indicated that Hep. 2 cell can produce a unique AP consisting of the heterodimeric form of placental and intestinal subunits.View full abstractDownload PDF (3433K)
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