SEIBUTSU BUTSURI KAGAKU

An atypical enzyme activity of L-aspartate: 2-oxoglutarate aminotransferase (GOT, EC 2. 6. 1. 1) was found in serum of a male patient (54 years old) with chronic hepatitis. The atypical GOT was migrated to a possition of slow β globulin by electrophoresis. The molecular size of the atypical GOT was approximately estimated 330, 000. Since the atypical GOT was fixed by specific antisera against IgG and λ light chain, the enzyme was found to be a complex of GOT and IgG (λ). The GOT-linked IgG was recognized to have an affinity for s-GOT, but not for m-GOT. The atypical GOT was slightly activated (131%) by 100μM pyridoxsal-5-phosphate, and this percentage was mostly agreeable to that of the patient GOT which was not linked to IgG (132%).

View full abstract

Show abstractHide abstract

The electroimmunofixation sandwich method is described as a simple, clear and accurate technique for a reconstruction test of isoenzymes and enzyme-linked immunoglobulins. The procedure is; the isoenzymes in an enzyme specimen are separated by electrophoresis, and previously prepared enzyme-linked immunoglobulin is layered on the support media. The media are incubated at 26°C for 1h, and complexes of the isoenzyme and the enzyme-linked immunoglobulin are formed. Since these complexes are soluble type, anti-immunoglobulin antibody is layered on the media. During the second incubation at 26°C for 2h, insoluble complexes of the isoenzyme, the enzymelinked immunoglobulin and the anti-immunoglobulin antibody are formed. Then, the support media are deproteinized, and enzyme staining is performed. Free isoenzymes which are not bound with the enzyme-linked immunoglobulin are removed by the deproteinization because the enzymes are not fixed on the media. From the patterns, the enzyme-linked immunoglobulin is found to have an affinity for the isoenzymes remaining on the media. This method was applied to the GOT-linked IgG (λ), amylase-linked IgA (λ) and LDH-linked IgA (λ), and satisfactory data were resulted.

View full abstract

Download PDF (2780K)

The mean contents of 24 hours urinary excretions of immunoglobulin and immunoglobulin fragments in normal subjects were 3.14mg, 1.23mg and 2.20mg for IgG, Fc and L-chain respectively. The mean contents of 24 hours urinary excretions of immunoglobulin and immunoglobulin fragments in myelogenous leukemia were 2.87mg, 0.81mg and 3.94mg for IgG, Fc and L-chain respectively. After chemotherapy the patients showed a decrese of serum IgG level associated with increased urinary excretions of Fc and L-chain.
From these observations, metabolism of immunoglobulin in myelogenous leukemia and its change by chemotherapy were discussed.

View full abstract

Register with J-STAGE for free!