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Biomedical subjects

K Ohga

Publications and source records attributed to K Ohga.

33 records · Page 2Linked to original sources

Ultrastructural studies of peripheral blood of neonates with Down's syndrome and transient abnormal myelopoiesis.

Ultrastructural studies were performed on blood samples from five neonates with Down's syndrome and transient abnormal myelopoiesis (TAM). Three methods of fixation were employed to detect diaminobenzidine (DAB) reactivity. The first method used glutaraldehyde solution, while the second and third methods used tannic acid-glutaraldehyde mixtures. Before fixation by the second method, specimens were washed in order to eliminate plasma, and before fixation by the third were diluted to lessen the effects of plasma protein. The latter two methods were more sensitive than the first for detection of DAB reactivity, while the third also resulted in better preservation of morphology than did the second. Even the first method was able to detect DAB reactivity in cells of megakaryocyte-platelet series in appropriate sections. Although the majority of blasts appeared with light microscopy to be undifferentiated, their ultrastructural morphology and ultrastructural cytochemistry were in fact found to be quite heterogeneous, consisting of cells of the megakaryocyte-platelet and granulocytic series, including basophils, and erythroid precursors. This finding supported the view that TAM was the result of unstable hematopoiesis rather than true leukemia.

3,3'-Diaminobenzidine↗

Hyperunstable hemoglobin Koriyama anti-Hb Gun Hill insertion of five residues in the beta chain.

A new hyperunstable hemoglobin was found in a Japanese girl who had very severe, chronic hemolytic anemia. Her parents and siblings were hematologically normal. The abnormal hemoglobin comprised a very small proportion of the total hemoglobin, although it was produced almost at the same rate as normal hemoglobin. Sequencing of an abnormal peptide which was liberated from the beta chain by hydrolysis with a protease from Staphylococcus aureus V8 disclosed the tandem insertion of a five-residue segment which included the proximal histidine at beta 92(F8).

Amino Acid Sequence↗

Radioimmunoassays for the thymic hormone serum thymic factor (FTS).

Four radioimmunoassays (RIA) are described for the quantitation of serum thymic factor (facteur thymique serique, FTS), a thymic peptide hormone. Each assay employs an antibody specific for FTS, synthetic FTS (Glp-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn) as the hormone standard, and a radioiodinated FTS analogue as the tracer. Since FTS lacks a tyrosine residue, 2 FTS analogues were synthesized by the solid-phase method with tyrosyl-alanyl or 3-(2,6-dichlorobenzyl)tyrosyl-alanyl in place of the amino-terminal pyroglutamyl residue (Glp). They showed full FTS immunoreactivity and their radioiodinated derivatives served as FTS tracers. Two assays used the antiserum from a rabbit immunized with an FTS-protein conjugate. Two other assays used a monoclonal antibody against FTS produced by a hybridoma derived from mouse myeloma cells and splenocytes from a BALB/c mouse immunized with an FTS-mouse IgG conjugate (Ohga et al., 1982). All 4 RIAs were specific for FTS. The more sensitive rabbit antiserum can detect as little as 1 pg of FTS in a 50 microliters sample, which may allow quantitation of the FTS circulating in human peripheral blood.

Amino Acid Sequence↗

Generation of a monoclonal antibody against facteur thymique serique (FTS).

A monoclonal antibody against one of the thymic hormones, facteur thymique serique (FTS), was generated by hybridization between mouse NS-1 myeloma cells and BALB/c splenocytes, the latter obtained from BALB/c mice immunized with synthetic FTS coupled to mouse IgG. Enzyme-linked immunosorbent assay (ELISA) was developed and employed to detect the hybridoma secreting specific antibody. The monoclonal antibody (MA-FTS) was highly specific for FTS and did not cross-react with other thymic hormones or other unrelated peptides. MA-FTS could recognize FTS (or FTS-like molecule) in human serum and could absorb completely the FTS-like activity from human serum.

Animals↗