A new method of graphic representation of properties of isotachophoretic boundary of anions was devised. The method is based on the characteristics of the boundary that concentration of the trailing ion is proportional to that of the leading ion and concentration of the common ion in the trailing phase is a linear combination of that of the leading ion and the common ion in the leading phase. Because of these characteristics, plot of a property of an isotachophoretic boundary, e.g., pH of the leading phase, pH of the trailing phase etc., versus the common ion concentration to the leading ion concentration ratio of the leading phase gives a single curve irrespective of the leading ion concentration. A graph showing various properties of an isotachophoretic boundary thus obtained gives guidelines for utilizations of the system to disc electrophoresis, stacking experiments and so forth.

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Concentration of acute phase reactants such as α₁-antichymotrypsin (ACT), α₁-antitrypsin (AT), α₁-acid glycoprotein (AG) and C-reactive protein (CRP) in serum and those except CRP in cerebrospinal fluid (CSF) were determined in Alzheimer's disease (AD) and other neurological disorders. Concentrations of these acute phase reactants except AT in serum were significantly high in AD as well as other diseases as compared with control. Alb quotient values {(alb in CSF/alb in serum)×1000} were significantly high in AD. Concentration of ACT, AT and AG in CSF were significantly correlated with alb quotient values in AD and other neurological diseases. These findings suggest that inflammatory process and also impairment of the blood-brain barrier were involved in AD.

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The incidence of anti-brush border antibodies (ABBA) in sera from patients with liver diseases, and extra-hepatic complications in ABBA positive cases were investigated. Further, apparent molecular weights of the target antigens of ABBA in liver diseases were analyzed by Westernblots in comparison with Heymann nephritis. ABBA were found in 12% of patients with liver diseases, and the highest incidence of ABBA was found in patients with chronic hepatitis C. The titre of ABBA in liver diseases was ranged from 20 to 160. The main extra-hepatic complications of patients with liver diseases positive for ABBA were chronic gastritis, cholelithiasis and renal dysfunction. However, there were no significant differences of extra-hepatic complications between ABBA positive and ABBA negative cases. There was a heterogenecity of the target antigens of ABBA. Sixty-four kD protein of brush border antigen (BBA) from rat small intestine and 44kD protein of BBA from rat kidney were found to be common target antigens of ABBA in liver diseases as well as in Heymann nephritis.

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Polyclonally increase of immunoglobulins were detected by agarose gel electrophoresis or immunoelectrophoresis in the serum of a patient with autoimmune hepatitis. However, the precipitation line of albumin on immunoelectrophoresis in the patient serum was extended to gamma area. By gel filtration, small amount of albumin was eluted in the fraction of high molecular weight, and by Protein G affinity chromatography, slight amount of albumin was adsorbed by Protein G with IgG. Moreover, a IgG-κ type M-component was revealed in the sample obtained after ion exchanged chromatography. On immunoelectrophoresis, the precipitation line of albumin in the fraction containing the IgG-κ type M-protein was extended to gamma area as the patient's serum. The purified IgG from the patient's serum treated with an acid, was able to recombine with normal human serum albumin and bovine serum albumin. Localization of the binding activity on IgG molecule was proved in the Fab region. There is a possibility that the IgG-κ type M-protein can have antibody like activity to albumin.

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1) The ultrafiltration of serum collected from dogs by a filtration film with a pore size of 300, 000, Blue Sepharose CL-6B affinity chromatography and Ultrogel AcA 22gel filtration chromatography eluted a third protein fraction in addition to α₁-macroglobulin (α₁-M) and α₂-macrogrobulin (α₂-M). The subsequent use of preparative agarose gel isoelectric focusing with a cover gel facilitated the extraction of pure α₁-M and α₂-M protein fractions.2) Analytical agarose gel isoelectric focusing and Ferguson plot by agarose gel electrophoresis revealed the following: (1) dog α₁-M had an isoelectric point (pI) of 5.4 and a molecular weight of 724, 000; and (2) dog α₂-M had a pI of 5.7 and a molecular weight of 758, 000.

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