SEIBUTSU BUTSURI KAGAKU

Clinical studies of serum immunoglobulins II

Serum immunoglobulin and transferrin levels in renal diseases

Hiromichi Sugiyama, Akio Kuroha, Hideaki Saito

1970 Volume 15 Issue 2 Pages 135-141
Published: August 30, 1970
Released on J-STAGE: March 31, 2009

DOIhttps://doi.org/10.2198/sbk.15.135

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The levels in serum of transferrin and immunoglobulins were studied in the patients with renal diseases. The concentration in the sera were measured using a modification of the radial diffusion method of Mancini et al.
The results were as follows:
1) The serum transferrin concentration in the patients with subchronic nephritis, nephrotic syndrome, chronic nephritis and the patients under artificial dialysis was lower than normal.
2) The serum IgG concentration in the patients with subchronic nephritis, chronic nephritis and the patients under artificial dialysis was lower, and the lowest in nephrotic syndrome.
3) The serum IgA concentration in the patients under haemodialysis was normal. In the patients with subchronic nephritis and chronic nephritis, and in the patients under peritoneal dialysis, it was elevated. However, it was lowered in nephrotic syndrome.
4) The serum IgM concentration in the patients with subchronic nephritis was higher, and that in the patients with other renal diseases were normal.

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Studies on α₂-macroglobulin and trypsin-protein esterase activity

Mineo Kojima, Tatsuo Wakahara, Yasushi Aoki, Hiroshi Anodo, Keiten Mat ...

1970 Volume 15 Issue 2 Pages 143-148
Published: August 30, 1970
Released on J-STAGE: March 31, 2009

DOIhttps://doi.org/10.2198/sbk.15.143

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1) Fraction-I, which is a portion of serum prtoein separated by means of gel filtration using Sephadx G-200, formed a complex of trypsin-protein esterase (TPE) when treated with trypsin and did not lose its enzymatic activity. Mild anti-tryptic activity was also demonstrated in this fraction.
The ratio of the tryptic activity to the anti-tryptic activity was 5. It is considered that the existence of anti-tryptic activity is due to a loss of enzymatic activity caused by the formation of the complex.
2) The esterase activity of α₂M-enzyme complex in serum was studied with the use of α-N-benzoyl-DL-arginine-p-nitroanilid HCl (BAPNA) as the synthesized substrate in human subjects. It was found that the serum protein, which had esterase activity, could be absorbed by anti-α₂M rabbit serum immunochemically. This complex could also protect trypsin esterase activity from soybean trypsin inhibitor. Moreover, our data suggested that one mole of α₂M was bound to two moles o trypsin.
3) In 83 patients with various diseases, the values of serum TPE activity were compared with those of serum α₂M measured by an immunological method. The result, that the correlation coefficient between the two values was 0.95 showed the greatly significant relation of TPE activity to α₂M level in serum. Accordingly, the measurement of α₂M concentration in serum can be replaced by the determination of serum TPE activity, which is a simpler technique.

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Purification of anti-H(O) agglutinin of eel serum by Disc electrophoresis

Hideo Sawada, Shoichi Yada

1970 Volume 15 Issue 2 Pages 149-153
Published: August 30, 1970
Released on J-STAGE: March 31, 2009

DOIhttps://doi.org/10.2198/sbk.15.149

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A method for the purification of anti-H(O) agglutinin of eel serum utilizing preparative Disc electrophoresis apparatus was described. The purified hemagglutinin showed a single band on starch gel electrophoretic analysis. In the analytical ultracentrifuge, the agglutinin had an s⁰_{20, w} value of 6.2 S, and was found to be inhibited weakly by human group OSe saliva. The minimum agglutinating dose against human O group red cells was around 0.2μg/ml.

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Studies on cartilaginous enzymes, degrading protein-polysaccharide complex

A simple electrophoretic method for estimating the enzyme activities and its application to the purification of the enzymes from puppy articular cartilage

Masaki Shiono

1970 Volume 15 Issue 2 Pages 155-163
Published: August 30, 1970
Released on J-STAGE: March 31, 2009

DOIhttps://doi.org/10.2198/sbk.15.155

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The light fraction of protein-polysaccharide complex (PPL) was isolated from bovine nasal septum. The enzymic degradation of PPL by protease (trypsin) or polysaccharidase (testicular hyaluronidase (HAse)) was apparently demonstrated by paper electrophoresis (Beckman No. 320046 paper strips, length 7cm, pH, 8.6, 0.05M borate buffer, 60V, 30min), followed by toluidine blue staining. Under these conditions, PPL remaind at the starting line, while the protease-degraded polysaccharide chains migrated towards anode as a broad band. HAse digestion, however, yielded two or three bands which were different in shape and mobility from that of the protease digestion products. Applying the paper electrophoretic method for estimating the activities, the PPL-degrading enzymes were purified from puppy articular cartilage minces by water extraction, protamine treatment, Sephadex G-75 gel filtration, and electrofocusing (pH 3-10), successively. There were separated HAse- and protease-type enzymes with isoelectric points of 5.8 and 7.6, respectively. These enzymes exhibited the optimum pH at about 3-4. The present method was shown to be advantageous with respect to its simplicity, applicability to micro-quantity of the sample, and reliable discrimination between protease- and HAse-type enzyme activities.

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A simple electric method of washing in staining procedure of Disc electrophoresis

Kazuo Shimao

1970 Volume 15 Issue 2 Pages 165-169
Published: August 30, 1970
Released on J-STAGE: March 31, 2009

DOIhttps://doi.org/10.2198/sbk.15.165

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