Serum-immunoglobulin (Ig) and complement (C₃) levels of 70 patients with liver cirrhosis and acute/chronic hepatitis were studied in comparison with those in 133 cases with a variety of allergic disorders. In liver cirrhosis, especially in advanced cases, an increase in IgG, A, M, D and E concentrations was observed.
A rise in IgE level in liver cirrhosis, the greatest among liver diseases, was almost the same as that in reaginic asthma and larger than that in allergic rhinitis and urticaria, while smaller than that in atopic dermatitis. C₃ level decreased in cirrhosis, especially in advanced cases. In cirrhosis, Ig levels increased as the disease advanced, and reduced in convalescence. In chronic hepatitis, although alterations of IgM, D and E were insignificant, there appeared an increase in IgG, and A. In acute hepatitis Ig levels were not elevated. C₃ concentration fell in severe acute hepatitis and slightly decreased in active chronic hepatitis.

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A new colorimetric method is presented for the assay of serum GPT activity on the basis of selective determination of pyruvic acid produced in the enzyme reaction under its optimal conditions by means of a modified procedure of the previously established method for the determination of the acid with p-dimethylaminobenzaldehyde. The method gives reliable results and is simple to be performed, and suitable to assay a large number of samples with a wide range of activity at the same time.
The outline of the standard assay procedure is as follows: 0.5ml of the substrate (10μ moles of 2-oxoglutaric acid and 100μ moles of DL-alanine) is mixed with 0.1ml of sample serum and incubated at 37° for 30 min. At the end of the incubation time, 1.0ml of 0.5% p-dimethylaminobenzaldehyde dissolved in an aqueous dimethylsulfoxide (60% by volume) is added to the reaction mixture to stop the enzyme reaction. The resulting mixture is mixed with 3.0ml of 12% potassium hydroxide solution with cooling, warmed at 37° for 45min. to develope the color, cooled and then diluted with 5.0ml of water. The absorbance of the final mixture at 420nm is read against the serum blank prepared in the same manner without the incubation. The enzyme activity expressed in the international units (μ moles of pyruvic acid formed/min,/1000ml of serum) is read on the calibration curve, which is prepared by treating 0.5ml portions of sodium pyruvate standard solutions and 0.1ml of 7.8w/w % bovine serum albumin (fraction No.V) solution or serum with very low GPT activity in the same way as described above without incubation.

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With the aid of the molecular sieve membrane, serum was separated into protein and non-protein parts in intact state and some clinical analyses were attempted in comparison with chemical methods of removal of protein. It was found that the analytical values of uric acid and creatinine in serum were completely satisfactory. However, some constituents in serum which are presumed to combine with protein showed considerably lower values when analyses were made with the present method.

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A new enzymatic method is proposed for the determination of lecithin in serum.
The principle of this method is as follows: Lecithin is hydrolyzed into diglyceride and phosphorylcholin by phospholipase C. When treated with lipoproteinlipase (Psedomonase fluorescens), triglyceride in serum and diglyceride produced by hydrolysis of lecithin are hydrolyzed into glycerol and free fatty acid. Glycerol produced by this procedure is transformed to pyruvate in the presence of glycerol-kinase, pyruvate-kinase, ATP and phosphoenolpyruvate. Being reacted with hydrazine, pyruvate forms hydrazone which shows the maximum absorbance at 450nm under the basic condition. Glycerol derived from triglyceride is determined by LPL-hydrozon method reported previously. And glycerol from lecithin fractions is calculated by subtracting glycerol derived from triglyceride fractions from the total values.
The amount of lecithin is calculated according to a certain formula from the value of optical density obtained at 450nm.
The precision of the method was also satisfactory.
Since the enzymatic method is simple and more specific for measurement of lecithin in comparison with the chemical and ALPase method. The former method is suitable for lecithin estimation in clinical laboratory.

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