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About 2-μm-sized polystyrene (PS) particles having uneven surfaces were prepared by a posttreatment in which toluene-swollen PS particles were thrown into a methanol bath to release toluene therefrom rapidly. The posttreatment was named the “solvent-absorbing/releasing method”. The PS particle had large dents at the surface. The size of the dents was changed by the conditions of the posttreatment.

AbstractHydroponically grown forty-day-old spinach (Spinacia oleraceaL.) plants (two cultivars, Okame and Lead) were exposed to 13CO2 for 6 hours in the light using a steady state 13CO2/12CO2 feeding system. The 13C incorporation into sugars, organic acids, amino acids, ascorbic acid, and oxalic acid in leaf blades, petioles and roots was measured at 3 and 6 hrs 13CO2: feeding, and the relative specific activity (RSA. 13C abundance of metabolites/ 13C abundance of atmospheric 13CO2 in the chamber) was calculated. The RSAs of the sugars were 40.7% and 35.1% at 3 In s and 47.7% and 46.3% at 6 hrs and those of the ascorbic acid were 7.0% and 6.7% at 3 hrs and 14.0% and 12.4% at 6 hrs in the leaf blades of Okame and Lead, respectively. The RSAs of oxalic acid were 2.3% and 2.3% at 3 hrs and 4.9% and 4.4% at 6 hrs in the leaf blades of Okame and Lead, respectively. The 13C incorporation into the metabolites of the petioles and roots was also investigated. Ascorbic acid was synthesized from currently fixed C and partly from the reserved C. Oxalic acid synthesis was active in the leaf blades, but less active in the petioles and roots. Nitrate reduction, oxalic acid synthesis and amino acid synthesis occurred simultaneously in the leaf blades.

A new type of gamma Gly-268 (GGA) to Glu (GAA) substitution has been identified in a homozygous dysfibrinogen by analyses of the affected polypeptide and its encoding gene derived from a 58 year-old man manifesting no major bleeding or thrombosis. The functional abnormality was characterized by impaired fibrin assembly most likely due to failure to construct properly aligned double-stranded fibrin protofibrils. This presumption was deduced from the following findings: (1) Factor XIIIa-catalyzed cross-linking of the fibrin gamma-chains progressed in a normal fashion, indicating that the contact between the central E domain of one fibrin monomer and the D domain of another took place normally; (2) Nevertheless, factor XIIIa-catalyzed cross-linking of the fibrinogen gamma-chains was obviously delayed, suggesting that longitudinal association of D domains of different fibrin monomers, ie, D:D association was perturbed; (3) Plasminogen activation catalyzed by tissue-type plasminogen activator was not as efficiently facilitated by polymerizing fibrin monomer derived from the patient as by the normal counterpart. Therefore, gamma Gly-268 would not be involved in the 'a' site residing in the D domain, which functions as a complementary binding site with the thrombin-activated 'A' site in the central E domain, but would be rather involved in the D:D self association sites recently proposed for human fibrinogen. Thus, the gamma Glu-268 substitution newly identified in this homozygous dysfibrinogen seems to impair proper alignment of adjacent D domains of neighboring fibrin molecules in the double-stranded fibrin protofibril, resulting in delayed fibrin gel formation.