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Volume 51 (2007)
- Issue 4 Pages 223-
- Issue 3 Pages 153-
- Issue 2 Pages 83-
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Volume 51, Issue 4
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Symposium
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Kiyotaka Fujita2007 Volume 51 Issue 4 Pages 223-226
Published: 2007
Released on J-STAGE: December 04, 2009
JOURNAL FREE ACCESSSome cases with abnormal laboratory data which is not related to the disease have been reported. The reason which appears the abnormal laboratory data are : ① interaction between immunoglobulins and other serum proteins, ② reaction with assay reagents, ③ nonspecific reaction by heterophil antibody, ④ association with antibody activity, ⑤ difference of reactivity between antisera and subclass of immunoglobulins. About this abnormal reaction, the immunochemical characterization, clinical significance, and laboratory detection of abnormal data are introduced.
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Masahiko Shigemura, Takanori Moriyama2007 Volume 51 Issue 4 Pages 227-230
Published: 2007
Released on J-STAGE: December 04, 2009
JOURNAL FREE ACCESSThere have been several reports describing a notable hyperamylasemia in patients with multiple myeloma. Such amylase-producing myelomas have been mainly described in the context of concomitant with salivary-type hyperamylasemia and with sialyl salivary-type amylase identified in a portion of those cases. Sialyl salivary-type amylase, with an abnormal anodic migration, was detected by isoamylase electrophoretic analysis. The abnormal isoamylase bands migrated toward the anode faster than the salivary isoamylase band (S2). The isoamylases were showed sensitive by neuraminidase treatment and were reacted with anti-human salivary monoclonal antibody. The isoamylases could be separated from residual normal isoamylase by using gel permeation chromatography. This paper reports the clinical laboratory findings indicating of sialyl salivary-type amylase in a patient with multiple myeloma.
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Yoshimasa J. Aoki, Mitsuaki Kameko, Kiyotaka Fujita, Yuzo Kayamori, Do ...2007 Volume 51 Issue 4 Pages 231-235
Published: 2007
Released on J-STAGE: December 04, 2009
JOURNAL FREE ACCESSWe observed a patient with IgG4-λ type M-proteinemia whose serum albumin (ALB) value elevated higher than total protein concentration (TP). The patient’s serum showed abnormality in not only ALB but also direct bilirubin (D-Bil) and iron (Fe) with an automated chemical analyzer. Blood chemistry findings were: TP 8.8 g / dl; ALB 9.2 g / dl; D-Bil –6.2 mg / dl; and Fe 25 μg / dl. The measurements of ALB, D-Bil, and Fe by automated chemical analyzer showed abnormal time course in the reaction and the precipitates were formed by the interaction between the patient’s serum and each reagent. Immunofixation electrophoresis revealed that these precipitates were the IgG4-λ type M-protein. The purified patient’s IgG4 molecules were found to be composed of two γ4 chains of 55 kDa and two λ chains of 24 kDa by Western Blotting analysis. To be common to three reagents was used to acidic buffer solution, approximately pH 4.0. Therefore, it is thought that the precipitates are occurred under the acidic conditions. This phenomenon may be caused by amino acid composition in the variable region or glycosylation of M-protein rather than conformational abnormality such as deletion of a domain in the constant region.
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Hirohisa Sato, Mariko Kudo, Yasushi Mariya, Minoru Yasujima, Kiyotaka ...2007 Volume 51 Issue 4 Pages 237-241
Published: 2007
Released on J-STAGE: December 04, 2009
JOURNAL FREE ACCESSTwo cases with abnormal laboratory data due to the presence of monoclonal proteins belonging to minor subclasses are described.Case 1 was a patient with IgA-κ type M-protein. The monoclonal IgA value as determined by serum protein electrophoresis was 6,450 mg / dl, while the serum IgA concentration was 4,310 mg / dl by turbidimetric immunoassay. Immunoelectrophoresis of the patient serum showed double IgA precipitate lines. We identified that the M-protein in this patient as the IgA2m(1) allotype by immunofixation electrophoresis using anti-IgA subclass antisera and SDS-PAGE without 2-mercaptoethanol.Case 2 was a patient with IgG-κ type M-protein. The monoclonal IgG was found to have mobility to α2 region. The γ-globulin fraction in this patient as determined by serum protein electrophoresis was 630 mg / dl, while the serum IgG concentration was 1,370 mg / dl by turbidimetric immunoassay. Immunofixation electrophoresis using anti-IgG subclass antisera revealed that this M-protein was the IgG4-κ type.In both cases, M-proteins belonging to minor subclasses may cause abnormal reactions in immunochemical determination.
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Jinko Ishikawa, Masato Maekawa2007 Volume 51 Issue 4 Pages 243-246
Published: 2007
Released on J-STAGE: December 04, 2009
JOURNAL FREE ACCESSAlterations in the serum lactate dehydrogenase (LD) isozyme pattern can serve as an indicator of pathologic conditions and cancer development. There have been some reports of unusual LD electrophoretic isozyme patterns. An abnormal electrophoretic pattern may result from additional LD fractions, altered mobility, altered molecular structure, or distortion of one or more normal bands. Distortion of normal bands may be caused by immunoglobulin or other protein binding, genetic variants, and tumor production. In routine laboratory, abnormal LD isozyme pattern with high serum LD activity is frequently due to LD-linked immunoglobulin. Its identification method is established. Here we describe clinical patients we encountered whose LD isozyme pattern is abnormal due not to immunoglobulin binding: extra band between LD1 and LD2 due to LD-α-lipoprotein complex and shifted LD isozyme pattern caused by reduced LD expression due to DNA methylation of LDHA or LDHB gene promoter region.
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