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Volume 30 (1986)
- Issue 6 Pages 387-
- Issue 5 Pages 323-
- Issue 4 Pages 247-
- Issue 3 Pages 151-
- Issue 2 Pages 91-
- Issue 1 Pages 19-
Volume 30, Issue 4
Displaying 1-10 of 10 articles from this issue
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Eiji Kajii, Yuhji Yamaguchi, Juichi Ueki, Yasusada Miura, Haruhiro Yos ...1986 Volume 30 Issue 4 Pages 247-250
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSOn the red blood cell membrane in a patient with autoimmune hemolytic anemia (AIHA) several glycophorin class blood group antigens were assumed to be acquired in relation to the disease. When the red blood cells were treated with Dispase, all of the acquired antigens were released to the supernatant in company with the native glycophorin class antigens and disappeared on the red blood cell membrane. Then a trial was made to analyze the supernatant of the red blood cell suspension with Dispase and the serum which contained the red cell autoantibody by capillary isotachophoresis. In each of the isotachopherogram, a specific peak which was not detected in the sample from normal human was found in the acidic zone. The protein substances expressed by these peaks will be available as a marker to diagnose AIHA because they are thought to be formed in association with AIHA.View full abstractDownload PDF (392K) -
Hideko Sakurai, Yuko Sudou, Hiromi Inage, Kotaro Watanabe, Akio Koyama ...1986 Volume 30 Issue 4 Pages 251-255
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSIn order to identify urinary proteins excreted from normal subjects, we employed a new method by which molecular weight and immunochemical property of urinary proteins can be determined simultaneously. Urine was subjected to linear gradient (3∼40%) SDS-PAGE and then transferred to nitrocellulose membrane by electrophoretic blotting method. The membrane was stained with Auro Dye and blotted proteins were identified by enzyme immunoassay using specific antibodies. In this method, we identified more than 12 protein bands from urine, that is, α2-macroglobulin, tubular epithelial antigen, Tamm-Horsfall glycoprotein, IgA, IgG, transferrin, albumin, α1-microglobulin, L-chain (dimer, monomer), retinol-binding protein, and β2-microglobulin. In addition, we found native forms and some fragments of immunoglobulins. In this report, we analyzed only normal subjects.
These results suggest that this method is useful for analysis not only of glomerular or tubular proteins but also tissue antigens from urine with various kinds of renal diseases.View full abstractDownload PDF (1613K) -
Mitsuharu Narita, Akio Koyama, Hideko Sakurai, Yuko Sudou, Hiromi Inag ...1986 Volume 30 Issue 4 Pages 257-263
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe urinary proteins from healthy adults were analyzed in different age groups, using gradient gel SDS-PAGE and electrophoretic blotting methods. The proportions of low molecular proteins increased as the age became elder, and this phenomenon began at fifties. Electrophoretic blotting analysis showed that the increased proteins were identified as retinol-binding protein, free-light chain (monomer and dimer), which were defined as tubular proteinuria.
From the above observations, we speculated that the increase in excretion of low molecular weight proteins by ageing, are mainly due to tubulopathy. This appear predominantly at fifties and gradually progress during ageing.View full abstractDownload PDF (2147K) -
Takatsugu Yamada, Hironobu Takada, Motoo Matsuda, Tetsuro Samata, Tosh ...1986 Volume 30 Issue 4 Pages 265-272
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSThe hemopexin from feline plasma was purified using a simple method and partially characterized. The purified hemopexin was recovered (about 13-23%) from Wheat germ Lectin Sepharose column by elution with 10% N-acetylglucosamine and judged to comprise 100% of the protein in the purified fraction by the analysis of immunoelectrophoresis and immunodiffusion. The feline hemopexin, with approximate molecular weight of 70, 000 was observed by Laemmli gel electrophoresis.
In order to partially characterize the purified hemopexin, first we carried out the analysis of amino acid composition. A profile of the composition showing essentially some similar features to that of human and rabbit before reported, was observed.
Secondaly, the levels of serum hemopexin during growth of cat were determined. A tremendous increase of the concentration was observed for 4 months after birth and the hemopexin have already attained to an adult level at 4 months. On the other hand, the total serum protein of cat increased slightly for the corresponding periods.
Moreover, the gene regulation of hemopexin during development of cat and the physiological function (s) were also described.View full abstractDownload PDF (2830K) -
Tsugikazu Komoda, Iwao Koyama, Kozue Okano, Masakazu Miura, Yoshikatsu ...1986 Volume 30 Issue 4 Pages 273-281
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSWe are re-evaluated here the characteristics of human urinary alkaline phosphatases (ALP).
According to the results of wheat germ agglutinin-affinity electrophoresis, serial lectin affinity chromatographies, isoelectric point, molecular weight determination, and immunological identification, the urinary ALPs from healthy adults and patients with hepatoma were similar to the natures of liver and/or bone like ALP. In the case of the patients with chronic nephritis or acute nephritis, the ALPs contained a major band of kidney like ALP with a minor band of bone and intestinal ALPs. But, the ALPs in pregnant woman had not only liver or bone ALP but also placental like ALP.
On the other hand, most of workers for urinary ALPs have been claimed that the molecular weight of urinary ALP is smaller than those of organic original ALPs. However, present data suggested that the molecular weight of urinary ALPs is well accorded to those of organic ALPs, except for the enzyme from the patient with acute nephritis. Moreover, total activity of the urinary ALP was close-related to that of the serum ALP.
Consequently, in general, urinary ALP may be derived from serum ALP by minor modification, suggesting that the excreated ALP in urine depend upon the half-life for respective ALP isozymes in blood stream.View full abstractDownload PDF (4731K) -
Nobuyuki Honma, Hiroshi Sugano, Fumitake Gejyo, Masaaki Arakawa, Giich ...1986 Volume 30 Issue 4 Pages 283-288
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSSerum ultrafiltrate was obtained from hemodialysis patients by using an extra corporeal ultrafiltration method equipped with a hollow fiber dialyser, and electrophoresed on the SDS-polyacrylamide gel having a high resolving power in the low molecular weight region. Among the major bands less than 40KD observed with plasma of hemodialysis patient, the bands of 29K, 28K, 25K, 22K, 16.7K and 8.9K molecular weights were also found in serum ultrafiltrate of the same patient. By an immunological method, the following bands were identified: α1-microglobulin (28K), retinol-binding protein (22K), prealbumin (16.7K) and β2-microglobulin (8.9K). As compared with serum ultrafiltrate obtained from healthy person, 28K, 25K (in some cases), 22K and 8.9K bands showed obvious increase in cases of hemodialysis patients except for one patient who showed an urine volume of 200ml/day and an electrophoretic pattern closed to that of healthy person.View full abstractDownload PDF (3721K) -
properties and changes in triathlon raceTakumitsu Hiro, Tsuyoki Kadofuku, Yoshiaki Makino, Tsuneo Sato, Hisao ...1986 Volume 30 Issue 4 Pages 289-294
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSA specific protein which appeared in plasma after a 10km-run was detected using two-dimensional electrophoresis, and it's properties were investigated. This specific protein was detected at almost the same position as albumin on two-dimensional gel under non-denaturing condition, but it was not adsorbed to anti-albumin-Sepharose column. The molecular weight was estimated to be 25, 000 on SDS-polyacrylamide gel electrophresis. This protein was stained with periodic acid-Shiff reagent but not with Sudan Black. This protein was also detected in triathlon race, but it's increase did not definite.View full abstractDownload PDF (5373K) -
Syuichi Tsuchida, Eiichi Nishiumi, Haruhiro Yoshida, Shigenori Ikemoto1986 Volume 30 Issue 4 Pages 295-300
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSHuman parotid salivary proteins were analyzed by micro-two-dimensional electrophoresis. Two variations were detected in the acidic salivary proteins and isoelectric points of these proteins ranged approximately from pH 3 to 5. The phenotypes of these polymorphisms were compared with that of polymorphisms reported for six systems, Pa, Pb, PmF, Pr, PIF and Ph. The results suggested that one of the acidic proteins examined was Pa system and the other was Pr system. In case of acidic salivary proteins, Pa and Pr systems could be separated by micro-two-dimensional electrophoresis, but PIF proteins could not adequately be separated by this method.View full abstractDownload PDF (357K) -
Hiroshi Sasaki, Mitsutaka Yoshida, Kei Furiya1986 Volume 30 Issue 4 Pages 301-308
Published: August 15, 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSLDH isoenzyme (s) linked to IgG of the lambda type found in the serum of a patient having had myocardial infarction is reported. This LDH-IgG complex has almost no enzymatic activity. It was found that the IgG of the patient acted as an inhibitor of LDH. LDH activity in normal human serum was inhibited and abnormal patterns of LDH isoenzyme (s) appeared when certain amounts of the patient's serum was added to a control serum as well as purified LDH isoenzymes. The IgG fraction in the serum was separated from the LDH-IgG complexes by 5'-AMP-Sepharose 4B column chromatography. Subclass analysis of IgG made it clear that the IgG in the serum was IgG3.View full abstractDownload PDF (4728K) -
1986 Volume 30 Issue 4 Pages 316
Published: 1986
Released on J-STAGE: March 31, 2009
JOURNAL FREE ACCESSDownload PDF (67K)
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