SEIBUTSU BUTSURI KAGAKU
Online ISSN : 1349-9785
Print ISSN : 0031-9082
ISSN-L : 0031-9082
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Volume 40, Issue 2
Displaying 1-6 of 6 articles from this issue
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  • Review Article
    1996 Volume 40 Issue 2 Pages 47
    Published: April 15, 1996
    Released on J-STAGE: March 31, 2009
    DOIhttps://doi.org/10.2198/sbk.40.47
    JOURNAL FREE ACCESS
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  • Instructive Lecture
    1996 Volume 40 Issue 2 Pages 48
    Published: April 15, 1996
    Released on J-STAGE: March 31, 2009
    DOIhttps://doi.org/10.2198/sbk.40.48
    JOURNAL FREE ACCESS
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  • Symposium
    1996 Volume 40 Issue 2 Pages 49-53
    Published: April 15, 1996
    Released on J-STAGE: March 31, 2009
    DOIhttps://doi.org/10.2198/sbk.40.49
    JOURNAL FREE ACCESS
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  • Plenary Session
    1996 Volume 40 Issue 2 Pages 54-76
    Published: April 15, 1996
    Released on J-STAGE: March 31, 2009
    DOIhttps://doi.org/10.2198/sbk.40.54
    JOURNAL FREE ACCESS
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  • Amyloidogenic property of murine serum amyloid A isotypes
    Toshiyuki Yamada, Yoshihisa Itoh, Tadashi Kawai, Barbara Kluve-Beckerm ...
    1996 Volume 40 Issue 2 Pages 77-81
    Published: April 15, 1996
    Released on J-STAGE: March 31, 2009
    DOIhttps://doi.org/10.2198/sbk.40.77
    JOURNAL FREE ACCESS
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    Serum amyloid A (SAA) is a precursor of amyloid A (AA), the fibrillar constituents in reactive amyloid deposits. In the murine model of reactive amyloidosis, an isotype of SAA (SAA2) forms fibrils, the other (SAA1) does not. We investigated the amyloidogenic properties of murine SAA isotypes using recombinant (r) proteins. rSAA2 was more soluble under neutral conditions and less soluble under the acidic conditions favorable for fibril formation than was rSAA1. When exposed to in vitro fibril-forming conditions in vitro, both isotypes formed materials that bound congo red and exhibited amyloid-like structures on electron microscopy, suggesting that SAA1 may also have a fibril-forming potential. It is important to note that SAA2 exists predominantly in preamyloidotic organ extracts. This may result not from the resistancee of SAA2 to proteolysis, as judged by manner of digestion by lysosomal proteases, but from a factor like preferential distribution of SAA2 in the organs.
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  • Rare types of LDH specific immunoglobulin G to isoenzymes
    Tatsuo Tozawa, Kyoko Adachi
    1996 Volume 40 Issue 2 Pages 83-88
    Published: April 15, 1996
    Released on J-STAGE: March 31, 2009
    DOIhttps://doi.org/10.2198/sbk.40.83
    JOURNAL FREE ACCESS
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    The immunoglobulins in LDH-immunoglobulin complexes differ in isoenzyme specificity, depending on the heavy chains and/or light chains. The specificities of IgA κ comprise two groups: 1) reactive against isoenzymes containing H2M trimer, 2) only against H2M2 tetramer. Those of IgG comprise three groups: 1) reactive against both H and M subunits, 2) only against M subunit, and 3) against isoenzymes containing H2 dimer. We studied seven patients with LDH-IgG complex and anomalous electrophoretic patterns of serum LDH isoenzymes, but different from those characteristic of usual LDH-IgG complexes. From reconstitution experiments, it appeared that isolated IgG from the patient was reactive against isoenzymes containing H2 dimer in 3 cases, H2M trimer in one case and H2M2 tetramer in 3 cases. The present study revealed that LDH-specific immunoglobulins have an affinity for LDH3 regardless of differencies in isoenzyme specificity. The finding suggests that LDH-specific immunoglobulins are antibodies with varying specificities to different structures in LDH3 molecule.
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