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T Kaidoh

Publications and source records attributed to T Kaidoh.

45 records · Page 3Linked to original sources
PubMed1984

Allotypes of murine factor B controlled by a locus within the S region of the H-2 complex.

Bf protein was directly precipitated from a mixture of EDTA-plasma from 13 different, inbred strains and rabbit IgG anti-mouse Bf, and was isolated by SDS-PAGE. The gel pieces containing Bf protein were digested by trypsin after labeling with 125I-Na, and then peptides of Bf protein with each mouse strain were compared by two-dimensional peptide mapping. The results for the peptide patterns with the standard B10 congenic strains (all of which Bf phenotypes had been already designated as Bf.1 because of the identical isoelectric point values) revealed two distinct peptide patterns. The peptide pattern of Bf protein appeared to be identical in each of the inbred strains, but only one of the 36 spots in the fingerprint observed either with B10 or B10.BR (designated tentatively as Bf.1 (b.k.) ) was not detected in that from B10.D2 and B10.S (designated tentatively as Bf.1 (d.s.) ). The results of peptide mapping with intra-H-2 recombinant inbred strains show that this structural variant was mapped to the S region, which is direct evidence that allotypes of murine Bf are encoded by a structural gene within the MHC.

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PubMed1981

Murine binding protein of the fourth component of complement: structural polymorphism and its linkage to the major histocompatibility complex.

The binding protein of the fourth component of complement (C4-BP) is a regulatory protein of the complement system with specific affinity for the fourth component. This paper describes a structural polymorphism of murine C4-BP and its linkage to the major histocompatibility complex of the mouse (H-2). After isoelectric focusing of whole mouse plasma in low-endosmosis agarose, C4-BP was demonstrated as a single precipitin band by overlaying monospecific antiserum on the agarose gel. Two C4-BP patterns were distinguished among many strains of mice on the basis of isoelectric point--C4-BP a type, which has a pH range of 6.5-7.0 (exemplified by B10.BR and B10.AKM), and C4-BP b type, which has a pH range of 6.3-6.6 (exemplified by B10 and B10.M). Genetic crosses between two strains bearing distinct C4-BP types demonstrate a C4-BP pattern representative of both types. A linkage study was carried out in which progeny of two backcross combinations--[(B10 X B10.BR)F1 X B10.BR] and [(B10.AKM X B10)F1 X B10.AKM]--were phenotyped for C4-BP type and serum fourth-component level. Results were obtained suggesting that C4-BP patterns are inherited by a single codominant locus (C4-Bp) linked to the H-2 complex. The recombination frequency between the C4-Bp locus and the S region was 0.017. By phenotyping appropriate intra-H-2 recombinants of three different backgrounds (B10, A, and HT), this locus was assigned to the right of the H-2D region.

Animals↗
PubMed1981

Murine C4-binding protein: a rapid purification method by affinity chromatography.

A simple, 3-step method was described for purification of murine C4 binding protein (C4-bp), a recently recognized serum protein that functions as one of the regulatory proteins of the complement system. The method consists of 1) affinity chromatography using TNBS-BGG-conjugated Sepharose beads, 2) gel filtration on a Sepharose 6B column, and 3) heparin-Sepharose chromatography. By this method, milligram quantities of C4-bp can be easily purified by more than 500-fold from EDTA-serum of various mouse strains, and the whole purification process can be completed within 1 wk. The overall yield of C4-bp is about 15%. The C4-bp thus prepared is homogeneous as judged by SDS-polyacrylamide gel electrophoresis and immunelectrophoresis. The purified mouse C4-bp showed physicochemical properties very similar to those described for human C4-bp. Like human C4-bp, mouse C4-bp is composed of several apparently identical subunits of the m.w. of 80,000. However unlike the human counterpart, the subunits of mouse C4-bp are not linked by disulfide bonds but are connected by non-covalent forces that can be disrupted by SDS. The purified mouse C4-bp retained binding affinity for C4 and showed unaltered antigenicity. Immunization of rabbits with the purified mouse C4-bp resulted in the production of potent and monospecific antisera.

Animals↗
PubMed1980

Structural polymorphism of murine C4 and its linkage to H-2.

Heretofore unrecognized structural polymorphism of murine C4(Ss) was demonstrated by using two different techniques: immunofixation electrophoresis and immunofixation isoelectric focusing. By these methods C4 was demonstrated as a broad protein band in freshly bled EDTA-plasma of inbred strains and wild mouse lines. Seven variants of C4(Ss) were identified among a large number of mice tested:C4-v (pI 7.7) exemplified by strain SM/J, C4-B(pI 7.5) exemplified by B10, C4-k (pI 7.3) exemplified by C3H/He, C4-bactrianus (pI 7.2) exemplified by Mus m.bacterianus, C4-d.s(pI 7.0) exemplified by DBA/2 and SJL/J, C4-castaneus (pI 6.6) exemplified by Mus m.castaneus, and C4-NC(pI 6.3) exemplified by NC. F1 hybrid exhibited two C4 bands, each of which corresponds to C4 of a parent. The possibility that the observed polymorphism represents variation of Slp was ruled out because an identical C4 pattern was always observed between male and female mice. The observed structural variation of murine C4 is controlled by a single codominant locus localized within or in the proximity of the S subregion of H-2. This was shown by phenotyping several intra-H-2 recombinant strains and backcross progeny, (B10 X NC)F1 X B10 and (B10 X NC)F1 X NC. An alloantiserum specific for one of the C4 variants (C4-NC) was successfully produced in C3H/He mice by repeated injection of purified C4 of NC mouse. This finding suggests that observed C4 variants or at least some of them represent antigenically distinguishable allotypes of murine C4.

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PubMedDate not supplied

Novel structure in the pellicular complex of Plasmodium falciparum gametocytes.

Using transmission electron microscopy, transverse dense bands were found to be associated with subpellicular microtubules and inner membranes in Plasmodium falciparum gametocytes. These dense bands may act as supportive structures to maintain the parallel arrangement of the microtubules, and/or to connect them to the inner membranes.

Animals↗
PubMedDate not supplied

Effect and localization of trifluralin in Plasmodium falciparum gametocytes: an electron microscopic study.

Trifluralin, a herbicide which is known to bind to plant and algal tubulin, induced ultrastructural changes in the microtubules of the mature Plasmodium falciparum gametocytes in vitro. Trifluralin treatment led to disassembly of the well ordered subpellicular microtubules, whereas it had no effect on microtubules of human platelets or of rat neuronal cells in vitro. The disassembled microtubules showed fragmented large tubular structures, which frequently were associated with the pellicular membranes. Electron microscopic autoradiography showed radioactive trifluralin associated with the microtubule fragments. These results provide evidence that trifluralin selectively binds to microtubules in malaria parasites and causes disruption of their structure.

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