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Biomedical subjects

E Ichikawa

Publications and source records attributed to E Ichikawa.

43 records · Page 3Linked to original sources
PubMed1985

Further resolution of human alpha-fetoprotein by affinity electrophoresis with erythroagglutinating phytohemagglutinin of Phaseolus vulgaris lectin.

Major molecular species of human alpha-fetoprotein(AFP), which were separated as single components by serial affinity chromatography with concanavalin A(Con-A) and Lens culinaris agglutinin, were further resolved into several bands by affinity electrophoresis with erythroagglutinating phytohemagglutinin of Phaseolus vulgaris lectin(E-PHA). Among the newly separated main molecular species, both Con-A- and E-PHA-reactive AFP(AFP-1X1) was demonstrated, contrary to the known sugar specificity of Con-A and E-PHA, in addition to molecular species of AFP reacting with Con-A but not with E-PHA(AFP-1X0) and of AFP reacting with E-PHA but not with Con-A(AFP-0X1). AFP-0X1 was formed from AFP-0X0, and AFP-1X1 from AFP-1X0 by neuraminidase treatment; thus, AFP-0X1 and AFP-1X1 represent asialylated and AFP-0X0 and AFP-1X0 sialylated molecular species. AFP-1X1' and AFP-0X0' were present as minor components. AFP-0X0' had no affinity for E-PHA, and the affinity increased in the order of AFP's-0X0(or 0X1), -1X1', -1X1 and -0X1. Proportions of those components varied depending on the pathophysiological conditions of AFP production.

Asialoglycoproteins↗
PubMed1985

Increased asialo-alpha-fetoprotein in patients with alpha-fetoprotein-producing tumors: demonstration by affinity electrophoresis with erythroagglutinating phytohemagglutinin of Phaseolus vulgaris lectin.

Affinity electrophoresis of human alpha-fetoprotein (AFP) with the erythroagglutinating phytohemagglutinin of Phaseolus vulgaris (E-PHA) gave up to five resolved bands (y, h, i, l and a; given in the order of decreasing affinity for E-PHA); band a having no affinity and bands y and h representing asialo-AFP's. The proportion of band y increased in extrahepatic tumors producing AFP, including yolk sac tumor, and of band h, in addition, in hepatocellular carcinoma. The proportion of either band y or h (or y + h) increased, over the means plus 2 standard deviations of the respective bands of cord serum AFP, in 20 out of 25 cases (80%) of hepatocellular carcinoma, including cell lines, and in all the patients with extrahepatic malignancy. Band i was detected in more than half the cases with malignancy, although the extent of its increases was much less. Band a appeared only in limited cases. None of the hepatitis and cirrhotic patients showed increased proportions of band y or h (or y + h), indicating the usefulness of the determination of asialo-AFP for the discrimination between benign and malignant liver diseases.

Adenocarcinoma↗
PubMed1984

Electrophoresis and electro-affinity transfer with specific antibodies to alpha-fetoprotein for detection of circulating immune complexes of alpha-fetoprotein.

A combination of agarose gel electrophoresis and a newly developed technique of electro-affinity transfer was applied to the detection of circulating immune complexes of human alpha-fetoprotein (AFP) and anti-AFP. After electrophoretic transfer to nitrocellulose membrane, to which affinity-purified polyclonal horse antibodies to human AFP were bound, the membranes were treated with or without rabbit immunoglobulins to human AFP, followed by overlaying with horseradish peroxidase-labeled goat anti-rabbit IgG for color development. Artificial complexes formed in vitro from human AFP and rabbit anti-AFP were clearly separated from free AFP by the agarose electrophoresis. The complexes were stained 20-40% as dark as the equivalent amount of free AFP by treatment with rabbit anti-AFP, and 10-20% as dark without the antibody treatment over a wide range of antigen-antibody ratios.

Animals↗
PubMed1983

Distinct molecular species of human alpha-fetoprotein due to differential affinities to lectins.

Resolution of human alpha-fetoprotein (AFP) into four distinct molecular species was demonstrated by a combination of two affinity chromatographies with crossed-immuno-affino-electrophoresis (CIAE) using concanavalin A (Con A) and Lens culinaris hemagglutinin (LcH)-A and LcH-B as affinity media. Of the four AFPs, AFP1 had no affinity for Con A, LcH-A, or LcH-B; AFP2 showed a high affinity for Con A, a low affinity for LcH-A, and an intermediate affinity for LcH-B (or a low affinity, depending on the lot of LcH-B preparations used); AFP3 revealed strong affinities for all of the three lectins; and AFP4, a trace component of hepatoma AFP in the present study, showed no interaction with Con A, but a definite interaction with LcH-A or LcH-B. These results were based on the determination of dissociation constants (Kd) of AFP-lectin complex by CIAE on isolated preparations of the three major hepatoma AFPs. These AFPs had identical electrophoretic mobilities of 0.86-0.87 (relative to human albumin) in the absence of lectins. The calculated mobilities of AFP2 and AFP3 were both reduced to 0.50-0.58 by saturation with lectins, but these two AFPs were clearly separated by 1 mg/ml LcH-A or LcH-B because of their large differences in Kd.

Carcinoma, Hepatocellular↗