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High-silicon composite casting blank with the silicon content of 12wt% in core layer and with the silicon content of 3wt% in coating layer was fabricated by composite casting. The high-silicon steel composite sheet with smooth surface and good shape can be obtained by hot rolling and warm rolling. After high temperature diffusion and pickling process, the composite sheet with thickness of 0.44mm and homogeneous silicon content of 5.8wt.% could be achieved finally. The test results of magnetic properties show that the magnetic induction intensity B50 and iron loss P15/50 are 1.778T and 2.892w/kg respectively. It implies that the high-silicon steel composite sheet with high magnetic induction and low iron loss can be prepared by composite casting and rolling process.

Summary??Protein engineering techniques were employed to graft the known anticoagulant Arg-Gly-Asp (RGD) motifcontaining sequences onto the surface of a mutant, inactive insulin framework. To probe the effect of a disulfide bond on the resultant anticoagulant activity, a native RGD-containing sequence from disintegrin dendroaspin, CFTPRGDMPGPYC, as well as a modified sequence, SFTPRGDMPGPYS were each examined. The peptide was placed between the C-terminal of the B chain and the N-terminal of the A chain and connected with B27 and A1 residues of the inactive insulin that lacks the characteristic intramolecular A6?11 disulfide bond within the A chain. The two RGD-containing insulin genes were over-expressed inE. coli, and purified and designated as RGD-Cys-Ins and RGD-Ser-Ins, respectively. Their amino acid compositions and mass data were in good agreement with those of expected. The RGD-Cys-Ins showed inhibition of platelet aggregation with an IC50of 3 ?M, while the latter was 3.5-fold less active. Thein vivoassay also indicated that the RGD-Cys-Ins had a higher activity in prolonging the bleeding time in mice than RGD-Ser-Ins. Both RGD-Cys-Ins and RGD-Ser-Ins retained about 25% of the proinsulin immunoactivity and had almost no insulin receptor binding activity. The results indicate the necessity for the RGD motif to be conformationally constrained for it to elicit a greater anticoagulant activity.

Protein engineering techniques were employed to graft the known anticoagulant Arg-Gly-Asp (RGD) motifcontaining sequences onto the surface of a mutant, inactive insulin framework. To probe the effect of a disulfide bond on the resultant anticoagulant activity, a native RGD-containing sequence from disintegrin dendroaspin, CFTPRGDMPGPYC, as well as a modified sequence, SFTPRGDMPGPYS were each examined. The peptide was placed between the C-terminal of the B chain and the N-terminal of the A chain and connected with B27 and A1 residues of the inactive insulin that lacks the characteristic intramolecular A6–11 disulfide bond within the A chain. The two RGD-containing insulin genes were over-expressed inE. coli, and purified and designated as RGD-Cys-Ins and RGD-Ser-Ins, respectively. Their amino acid compositions and mass data were in good agreement with those of expected. The RGD-Cys-Ins showed inhibition of platelet aggregation with an IC50of 3 μM, while the latter was 3.5-fold less active. Thein vivoassay also indicated that the RGD-Cys-Ins had a higher activity in prolonging the bleeding time in mice than RGD-Ser-Ins. Both RGD-Cys-Ins and RGD-Ser-Ins retained about 25% of the proinsulin immunoactivity and had almost no insulin receptor binding activity. The results indicate the necessity for the RGD motif to be conformationally constrained for it to elicit a greater anticoagulant activity.

Protein engineering techniques were employed to graft the known anticoagulant Arg-Gly-Asp (RGD) motif-containing sequences onto the surface of a mutant, inactive insulin framework. To probe the effect of a disulfide bond on the resultant anticoagulant activity, a native RGD-containing sequence from disintegrin dendroaspin, CFTPRGDMPGPYC, as well as a modified sequence, SFTPRGDMPGPYS, were each examined. The peptide was placed between the C-terminal of the B chain and the N-terminal of the A chainand connected with B27 and A1 residues of the inactive insulin that lacks the characteristic intramolecular A6-11 disulfide bondwithin the A chain. The two RGD-containing insulin genes were over-expressed in E. coli, and purified and designatedas RGD-Cys-Ins and RGD-Ser-Ins, respectively. Their amino acid compositions and mass data were in good agreement with those ofexpected. The RGD-Cys-Ins showed inhibition of platelet aggregation with an IC50of 3 μM, while the latter was3.5-fold less active. The in vivoassay also indicatedthat the RGD-Cys-Ins had a higher activity in prolonging the bleeding time in mice than RGD-Ser-Ins. Both RGD-Cys-Ins and RGD-Ser-Ins retained about 25% of the proinsulin immunoactivity and had almost no insulin receptor binding activity. The results indicate the necessity for the RGD motif to be conformationally constrained for it to elicit a greater anticoagulant activity.

The immunosuppressive effects of berbamine on murine immune functions were observed. The results showed that berbamine could significantly inhibit the proliferative response of spleen cells to ConA and LPS, reduce the amount of haemolytic plaque forming cells and also weaken the delayed type hypersensitivity (DTH) reaction and mixed lymphocyte reaction (MLR) induced by allogenic antigen. Furthermore, it showed that berbamine could decrease the ratio of CD4 positive cells to CD8 positive cells of spleen T lymphocytes by FACS assay which may be one of the mechanisms of the action of berbamine. © 1997 John Wiley & Sons, Ltd.

The immunosuppressive effects of berbamine on murine immune functions were observed. The results showed that berbamine could significantly inhibit the proliferative response of spleen cells to ConA and LPS, reduce the amount of haemolytic plaque forming cells and also weaken the delayed type hypersensitivity (DTH) reaction and mixed lymphocyte reaction (MLR) induced by allogenic antigen. Furthermore, it showed that berbamine could decrease the ratio of CD4 positive cells to CD8 positive cells of spleen T lymphocytes by FACS assay which may be one of the mechanisms of the action of berbamine. © 1997 John Wiley & Sons, Ltd.