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The purpose of this study is the analysis and the integrated design of sustainable EFB (empty fruit bunch) supply chain from pelletizing to exporting. In this study, Malay Peninsula is set to be as an analytical target place, supply chain of EFB pellets as a biomass derived from oil palm are analyzed in different cases. In order to grasp the difference of the whole system performance in cases, a simple mill case and multiple mill case are prepared. Cases include two cases “EFB concentrated processing case” and “EFB distributed processing case”. Supply chain is composed with three sectors, resource, supply and demand, and this study analyzes the supply sector. Processes of the supply sector are extract, transport, dry, pelletize and ship. By differing the layout of the dry process before and after transport in two cases, case 1-d and case 1-w, influence of the difference in water content of biomass is evaluated in each case. Based from the retail analysis, CO2 emission of EFB distributed processing case is 2.60 kg-CO2/GJ-pellet and resource utilization rate of this case is 62%. By substituting coal by EFB pellets, 0.08 t-CO2/GJ-pellet is reduced., Proceedings of the 26th European Biomass Conference and Exhibition, 14-17 May 2018, Copenhagen, Denmark, pp. 855-866

The composition dependence of the Yb valence and of the thermal expansion have been studied in the YbGa$_x$Ge$_{2-x}$ system. X-ray diffraction reveals that single-phased samples isostructural to YbGaGe are obtained in the range of 0.9, To appear in J. Alloys Compd

It has been reported that Nak(a)-negative platelets lack GP IV. To examine the GP IV genetic defects in Nak(a)-negative platelets, we studied four unrelated Nak(a)-negative subjects by amplifying their GP IV cDNA, which were synthesized from platelet mRNA using the reverse transcriptase/polymerase chain reaction (RT/PCR). We detected the entire coding region of GP IV mRNA in the platelets of all four subjects. Restriction enzyme analysis of the amplified GP IV cDNA showed fully predictable cutting sites. These results suggest that no gross deletion or insertion had occurred in the GP IV mRNA of Nak(a)-negative platelets.

Platelet membrane glycoprotein (GP) IIb carries not only the Baka alloantigen but also an autoantigen in some patients with chronic idiopathic thrombocytopenic purpura (ITP). We previously reported one ITP patient (RY) with anti-GPIIb autoantibody in her plasma. In this report, we investigated whether the epitope of the autoantigen on GPIIb (case RY) is identical to that of the Baka alloantigen or not. The anti-Baka antibody used in this study was obtained from a mother with a child suffering from neonatal alloimmune thrombocytopenic purpura as reported by Okada et al. Immunoblotting showed that the anti-Baka antibody bound to GPIIb from Baka-positive platelets only. In contrast, the anti-GPIIb autoantibody in RY plasma bound to GPIIb, irrespective of Baka phenotype. In addition, after neuraminidase treatment of GPIIb on nitrocellulose paper, the anti-Baka antibody failed to bind to Baka-positive GPIIb, while the autoantibody still bound to GPIIb. From these data, we conclude that the epitope of the autoantigen in RY patient is different from that of the Baka alloantigen.

We describe the membrane localization of a new platelet-specific alloantigen, designated Naka, that is involved in refractoriness to HLA-matched platelet transfusions. By indirect immunoprecipitation, anti-Naka antibody precipitated a single, radiolabeled platelet membrane protein with a molecular weight (mol wt) of 91 Kd from Naka-positive platelets. When radiolabeled Naka-negative platelets were used as a source of target antigens, no radiolabeled proteins were precipitated. The analyses using nonreduced-reduced two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and using rabbit antiglycoprotein (GP)IV demonstrated that this protein corresponds to GPIV (alternatively GPIIIb). Furthermore, in dot immunobinding, anti-Naka antibody bound to purified GPIV. Our results provide definitive evidence that the Naka alloantigen is carried on GPIV. These results also demonstrate that, on occasion, antibodies against GPIV may play an important role in refractoriness to platelet transfusions.

Male (NZW x BXSB) F1 (W/B F1) mice, which develop lupus nephritis, myocardial infarction, and thrombocytopenia, showed reduced platelet lifespan (PLS) and increased platelet-associated antibody (PAA) values. There were statistically significant correlations between the increase in PAA values and either the reduction in PLS or the decrease in platelet counts. This and the results of platelet transfer experiments between old male W/B F1 mice and either female W/B F1 or normal BALB/c mice indicate that PAAs on the platelet surface play a crucial role in the destruction of platelets in W/B F1 mice. The mechanism of thrombocytopenia observed here appears similar to that of human idiopathic thrombocytopenic purpura (ITP). Therefore, we think that W/B F1 mice are a potentially useful animal model for investigating the effectiveness and mode of action of therapeutic agents in human ITP, and that they may provide additional information on the basic mechanisms of this autoimmune phenomenon.

We investigated the location of platelet-specific alloantigen Baka on platelet membrane glycoproteins. In indirect immunoprecipitation experiments, the anti-Baka antibody precipitated glycoprotein (GP) II b and a small amount of GP III a. The immunoblots using partially purified GP II b/III a complex as the target antigen indicated that GP II b alpha carried the Baka alloantigen. When the partially purified GP II b/III a complex digested with chymotrypsin was examined, the Baka alloantigen was found on a 65 kD fragment derived from GP II b alpha under reducing conditions. In addition, the immunoblots after two-dimensional nonreduced-reduced SDS-PAGE directly indicated that the 65 kD fragment had a mol. wt. of 80 kD under nonreducing conditions. The immunoblots using platelets digested in situ with chymotrypsin indicated that the 65 kD fragment of GP II b alpha was retained by the platelet membrane. We conclude, therefore, that the Baka alloantigen is located on a 65 kD fragment that represents the membrane side of the cleavage site of chymotrypsin on GP II b alpha.