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Volume 43, Issue 3
Displaying 1-9 of 9 articles from this issue
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Tomoko Kubomi, Tuyosi Fujita, Yuhsi Matuo1999 Volume 43 Issue 3 Pages 129-138
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSFACE (fluorophore-assisted carbohydrate electrophoresis) is a method for the separation of fluorophore-labeled saccharides by the use of polyacrylamide gel electrophoresis. The method is characterized by high resolution, high sensitivity, and ease of use without expensive giant-sized machine such as mass spectrometry. It has been found to be useful for the analysis of oligosaccharides profiling of N-linked or O-linked glycans after releasing saccharides from glycoproteins and for sequencing oligosaccharides component. Judging from the importance of oligosaccharides in glycoproteins and the changes in oligosaccharides of cancer cell surface, the method described here is hopeful as a unique analysis tool in the field of basic medical science.View full abstractDownload PDF (3561K) -
Tatsuo Tozawa1999 Volume 43 Issue 3 Pages 139-145
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSIt has been proposed that the immunoglobulins in some naturally occurring macroamylases may primarily directed to animal amylase. This would suggest that there may also be an antibody to animal amylase with inability to bind endogenous amylases in circulation. On the basis of this assumption, an antibody to porcine pancreatic amylase (PPA) was investigated in sera from patients with inflammatory bowel disease (IBD): ulcerative colitis (UC) and Crohn's disease (CD), because serum antibodies to various dietary antigens have been demonstrated to be a significantly prevalent in patients with IBD. This investigation took advantage of the abilities of serum to inhibit specific activity of added PPA and to form an artificial macroamylase with the PPA. As expected, such antibodies to PPA were detected frequently in patients with CD (19/50, 38%), rarely in patients with UC (1/50, 2%) and not at all in normal controls (0/30). There were two different types of antibodies differing in their reaction with PPA; one was an enzyme-inhibiting antibody and another an enzyme-noninhibiting antibody. The former seemed to be of monoclonal or oligoclonal IgG whereas the latter was of polyclonal IgG and IgA or polyclonal IgG alone, and both were detected in almost cases. The presence of the antibodies specific for CD suggests that the antibodies may play an etiological role in CD, of which the etiology is still unknown.View full abstractDownload PDF (5055K) -
Mutsuko Kusanagi, Kiyotaka Fujita, Ikunosuke Sakurabayashi, Norikazu S ...1999 Volume 43 Issue 3 Pages 147-151
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe reaction of a human IgA1-κ type M-protein with cellulose acetate (Separax-SP) membrane is described. When a membrane consisting of diacetylcellulose and triacetyl cellulose (1:1) was used, the M-protein showed a reactivity with this membrane. The IgA1 molecules were found to have a molecular weight of 170, 000 and composed of two α1 chains of about 64, 000 and two κ chains of 23, 000. Since the patient's αFab and αFc alone can not induce reactions on Separax-SP, this suggests that the reaction of the M-protein with the membrane can not be ascrived to the antigen-antibody reaction. The possibility exists that the reaction between acetyl cellulose of the Separax-SP membrane and the patient's M-protein is due to a physical steric reactivity. The present case seems to be the first report of IgA1-κ type M-protein which reacts with Separax-SP membranes.View full abstractDownload PDF (5441K) -
Kinue Miyazima, Tadashi Hoshino, Yoko Yoshitomi, Kazumi Abe, Toshihiro ...1999 Volume 43 Issue 3 Pages 153-157
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSSalivary (S)-type amylase (AMY) variants (slow-S variants) which migrate slower than S1-AMY were identified by electrophoretically and named as slow-S1, slow-S2, and slow-S3 from anodal side. Briefly, the tested samples were incubated with or without anti-S-AMY inhibitory monoclonal antibodies, and the slow-S variants were indentified by checking the patterns of electrophoresis for the disappearance or reduction of those AMY bands. Slow-S1 was detected at the same position as pancreatic (P)2-AMY, slow-S2 at about the same position as dominant-P2S, and slow-S3 between P1-AMY and dominant-P2S. The detection rates of these bands were 0.07% (5/7, 234) for slow-S1, 0.17% (12/7, 234) for slow-S2, 0.03% (2/7, 234) for slow-S3, respectively. The cause of occurrence of these slow-S variants is not yet obscured. Further studies are warranted to determine whether hereditary factors, modification by the sugar chain or deamination is associated with occurrence of the slow-S variants.View full abstractDownload PDF (2455K) -
Toshihiro Watanabe, Hiroaki Sato, Yoshimasa Sagane, Yozo Nakazawa, Kat ...1999 Volume 43 Issue 3 Pages 159-164
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSPhospholipase D (PLD) was highly purified from cabbage leaves of three different cultivars. Each purified PLD showed a single protein band with molecular masses of 87 kDa on SDS-PAGE, respectively. Peptide maps of each purified PLD after digestion with Lysyl Endopeptidase or V8 Protease gave the same pattern of proteolytic peptide fragments. Previously, Pannenberg et al. suggested the existence of two isozymes designated as PLD1 and PLD2. The N-terminal amino acid sequences of whole PLD and of proteolytic peptide fragments were determined. As a result, the PLD isolated from cabbage leaves was identified as PLD2.View full abstractDownload PDF (7110K) -
Hiroshi Ihara, Natsuko Toya, Takashi Kakinoki, Asuka Tani, Yutaka Aoki ...1999 Volume 43 Issue 3 Pages 165-169
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSElectrophoretic separation and quantitation of serum proteins, including paraproteins, remain essential for the diagnosis and management of a variety of disorders. We examined the Beckman automated Paragon 2000 capillary zone electrophoresis (CZE) system and compared its electropherograms to those obtained by cellulose acetate electrophoresis (CAE). Within-run CVs using seven different capillaries and between-day CVs for CZE were <2% for albumin; they were <6% for α1-globulin, α2-globulin, β-globulin, and γ-globulin. From 2.7 to 15.0g/dl of total protein concentrations, the same electrophoretic patterns could be observed. Comparisons of the five principal bands obtained by CZE and cellulose acetate electrophoresis (CAE) gave correlation coefficients from 0.8 to 0.9. On a quantitative basis in 55 specimens, albumin by CZE was on average 10% lower than CAE, and α1-globulin and β-globulin were 93% and 15% higher than by CAE, respectively (p<0.001). Based on our use of the Beckman Paragon software and our reference values (percent of total protein) for CZE of 56.3 to 68.9% for albumin, 3.9 to 6.3% for α1-globulin, 4.8 to 8.4% for α2-globulin, 7.9 to 11.9% for β-globulin, and 9.9 to 21.5% for γ-globulin, we found 75% to 100% agreement with CZE; i.e., both methods gave either normal or abnormal results of the time. Patients showing a gammopathy gave values that were higher by CZE 60% of the time. Furthermore, the CZE system can resolve prealbumin, α1-acid glycoprotein, α1-antitrypsin, hemopexin, transferrin, and complement besides to the usual five bands.View full abstractDownload PDF (899K) -
Hidekazu Araki, Ayako Katagiri, Keiichi Sano, Takehide Matsuda, Toshio ...1999 Volume 43 Issue 3 Pages 171-175
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSAtypical bands are frequently found at cathode side than the band of apolipoprotein (apo) E4 isoforms separated by Phenotyping Apo E IEF System (Jokoh Co. Ltd.). Then, we developed to resolve the atypical phenotype bands as apo E5 and apo E7 isoforms by PCR with restriction fragment length polymorphism and with amplification refractory mutation system. From the results, the genetic identification of atypical apo E5 and apo E7 phenotype bands was well accorded to the apo E phenotypes separated by the Phenotyping Apo E IEF system.View full abstractDownload PDF (4115K) -
Kiyotaka Fujita, Mutsuko Kusanagi, Masaaki Arakawa, Ikunosuke Sakuraba ...1999 Volume 43 Issue 3 Pages 177-180
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSImmunofixation electrophoresis (IFE) is used routinely to identify monoclonal immunoglobulins (M-proteins) in serum and Bence Jones proteins in urine. A method for subclass typing of IgG and IgA type M-proteins using MINIFIXTM IFE kit is described in this paper. The antisera prepared for MINIFIXTM kit (IgG and IgA subclass sets), were used and M-proteins in 20 patient sera were analyzed. The subclass types of the M-proteins were identified as seven IgG1, one IgG2, two IgG3, seven IgA1, two IgA2 and one IgG1-IgA1 multi type. These results did not conflicted with those of western blotting analysis. The MINIFIXTM IFE kit is useful for identification of the subclasses of IgG and IgA type M-proteins. The MINIFIXTM IFE kit employs regular-sized agarose gels (102×77mm) but because of the reduced track width, will allow two patient samples per gel. Consequently, the MINIFIXTM IFE system offers excellent economy with each kit containing all the necessary reagents.View full abstractDownload PDF (4677K) -
Tetsuo Maeda, Mitsuo Maeda, Tatsuo Tozawa1999 Volume 43 Issue 3 Pages 181-183
Published: September 15, 1999
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA case of macroamylasemia occurring in a man and his daughter is described. A 65-year-old man who was hospitalized for hepatic dysfunction had persistent hyperamylasemia. The ACCR was low level. Serum amylase electrophoresis showed an abnormal broad band. The amylase elution pattern on a Sephadex G-200 column showed a macromolecular peak between 19S and 7S, indicating that the amylase had a larger molecular structure than that of normal amylase. An immunoprecipitate examination revealed the macroamylase to be an amylase linked to immunoglobulin A-λ. Serum amylase from the patient's healthy daughter showed the same characteristics as the patient, although amylase from the other members of his family did not. The etiology of naturally occurring macroamylasemia has not been resolved.View full abstractDownload PDF (2145K)
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