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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 3
Displaying 1-8 of 8 articles from this issue
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Its application to analysis of antigen-antibody interactionsKazusuke Takeo1993 Volume 37 Issue 3 Pages 141-146
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
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Tatsuo Tozawa1993 Volume 37 Issue 3 Pages 147-153
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSAmylase-producing tumors are mainly lung cancer, ovarian cancer and myeloma. The type of isoamylase produced by the tumors is exclusively of the salivary type (s-). Therefore, hyper s-amylasemia is a valuable aid in the diagnosis of amylase-producing tumors, however, occurs in a large variety of conditions. This paper reports the clinical laboratory findings indicating of presence of tumor amylase. One hundred and eighty sera from 85 patients with primary lung cancer and 185 sera from patients with hyper s-amylasemia, but not suffering from lung cancer, ovarian cancer or myeloma, were studied for the presence of tumor amylase by amylase activity measurement and isoamylase electrophoresis. A persistently increased value for amylase in serum and/or a S3 isoform/S2 isoform activity ratio of greater than 33% were a useful indicator of the presence of tumor amylase. An incidence of amylase-producing tumor of 7% among the 85 cases of primary lung cancer was found.View full abstractDownload PDF (4160K) -
Makoto Otsuki1993 Volume 37 Issue 3 Pages 155-158
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
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Masatoshi Ueda, Kazuhisa Taketa1993 Volume 37 Issue 3 Pages 159-164
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSPersistent hyperamylasemia is known to occur in patients with end-stage renal disease (ESRD). Isoamylase determination using two different methods revealed P-type hyperamylasemia in ESRD patients. The ratios of amylase clearance to creatinine clearance and S-type amylase clearance to creatinine clearance rose significantly in ESRD compared to controls. The ratio of P-type amylase clearance to creatinine clearance revealed no significant difference between ESRD and controls. Histological pancreatitis was found in 51.9% of the ESRD patients as compared with 14.8% in the controls. The pancreatitis was chronic in nature in 85.7% of the ESRD patients showing changes of pancreatitis. Secretin administration to additional group of 12 patients with ESRD failed to raise total and P-type serum amylase levels except one case. In conclusion, P-type hyperamylasemia is mainly due to impaired excretion of the isoamylase by the damaged kidney, rather than increased supply from the pancreas.View full abstractDownload PDF (614K) -
Michio Ogawa1993 Volume 37 Issue 3 Pages 165-169
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
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Kiyoshi Takatsuki, Hiromitsu Matsuzaki1993 Volume 37 Issue 3 Pages 171-174
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA patient with IgA lambda type multiple myeloma who appeared to be secreting salivary type amylase ectopically is reported. An amylase producing cell line, KHM-1B was established from the patient. Chromosome analysis of KHM-1B showed many qualitative and quantitative abnormalities including a translocation between 1p 13 or 21, near the amylase gene locus, and 9q 34, the abl oncogene locus. These finding suggest that the amylase gene in KHM-1B is activated by the translocation. A rearranged amylase gene was demonstrated by Southern blot analysis with only one enzyme, Accl. Since we reported the first case of amylase-producing myeloma, eleven other cased have been successively reported in the Japanese literature.View full abstractDownload PDF (2481K) -
Susumu Kurioka, Keiko Tomaru, Yasuyo Sato, Yasuyuki Kurosu1993 Volume 37 Issue 3 Pages 175-181
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSSeparation of 11 model proteins of various pI and MW values, and proteins in human serum, were performed by capillary electrophoresis using untreated fused silica capillary with 100mM sodium borate (pH10.0) for electrolyte and 100mM phosphoric acid (pH2.5) for washing the capillary between the run. Proteins in human serum were also separated into five fractions (albumin, α1, α2, β and γ-globulin) by the same conditions as above within 8min. The model proteins showed the migration time based on their pI values and the reproducibility of both the migration times and peak areas was good except for a few basic proteins.View full abstractDownload PDF (721K) -
Kiitiro Sitizyo, Takashi Takeuchi, Minoru Suzuki, Toshiyuki Saito1993 Volume 37 Issue 3 Pages 183-188
Published: June 15, 1993
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSBasic conditions of acid violet 17 staining was examined on the cellulose acetate membrane electrophoresis for domestic animals. Staining sensitivity of acid violet 17 was approximately 20 times more than ponceau 3R staining. This higher sensitivity allowed us to analyze specimens of urine at the concentration of protein as low as 40mg/dl. Acid violet 17 was a useful staining for the serum protein of cattle, pigs, dogs and chickens, but not for rabbits. The urinary proteins in healthy dogs and dogs with proteinuria were also demonstrated using the staining method with acid violet 17. According to the result, urine of healthy dogs contained 4∼14mg/dl protein, and urinary protein can be separated, albumin (14.4%), α∼β1-globulin (68.0%) and β2∼γ1-globulin (17.2%) by cellulose acetate membrane electrophoresis. The electrophoretic pattern of the dogs with proteinuria resembled with those of serum protein, indicating high contents of albumin. In addition, the urinary proteins of dogs with microfilaremia were characterized by a high content of β1∼γ-globulin and low molecular weight protein.View full abstractDownload PDF (1764K)
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