Objective Recent findings indicate that the serological and biochemical characteristics of porcine erythrocytes share many similarities with human red blood cell (hRBC). Scientists believed that humanized porcine red blood cells (pRBC) could be used as one alternative source for human blood transfusion. Methods In order to eliminate ?Gal antigen and non-?Gal on the surface of pRBC, recombinant soybean ?-Galactosidase (rS?-GalE) constructed by our lab was used to remove terminal ?Gal residues from ?Gal antigen, and mPEG-BTC was used to camouflage non-?Gal xenoantigen on the surface of pRBC. Results The carbohydrate structures of ?Gal xenoantigen of pRBC treated with rS?-GalE were completely modified. The antigenic determinants of ?Gal and non-?Gal xenoantigen on the surface of pRBC were successfully camouflaged through mPEG-BTC modification. But this modification needed higher concentration of mPEG-BTC which could cause slight structure damage. Considering this, with combination of ?Gal xenoantigen conversion by rS?-GalE and chemical camouflage of non-?Gal xenoantigen with lower concentration of mPEG-BTC, the antigenic determinants of pRBC were attenuated and hemagglutination were diminished.Conclusion The morphology, structures, functions and deformability of pRBC modified with rS?-GalE, mPEG-BTC and rS?-GalE+ mPEG-BTC were normal.

Objective: Soy products may cause excessive intestinal gas because of soybean oligosaccharides . The effect of recombinant ?-galactosidase on eliminating mouse flatus was observed. Methods:The mouse model of flatulence was set up by ig raffinose and stachyose and the flatulence was investigated by measuring intestinal flatulent volume. Oligosaccharides were examined by TLC test and soybean protein was examined by SDS-PAGE. Results: Raffinose and stachyose can result in mouse flatus and recombinant ?-galactosidase can eliminate it without any effect on soybean protein. Conclusion: Recombinant ?-galactosidase can eliminate flatus, and be used as food additive.

This study was aimed to establish the quality and quantity analysis methods of tectoridin contented in the Iris tectorum Maxim. Thin layer chromatography (TLC) method was used to give quality analysis on tectoridin in I. tectorum. And the HPLC method was used to give quantity analysis on tectoridin in I. tectorum. The Diamonsil C18 (200 mm í 4.6 mm, 5 μm) column was used as analytical column. The acetonitrile-0.2% phosphoric acid (20:80) was used as mobile phase at the flow rate of 1.0 mL·min-1. The detection wavelength was 265 nm and the column temperature was 25℃. The results showed that the quality analysis of I. Tectorum had specific identification with-out the interference of other ingredients. The amount of inlet tectoridin had a good linearity with the response val-ue of peak area in the range of 0.12~2.22 μg. The average recovery rate was 100.96%. It was concluded that this method was simple and reproducible, which can be used in the quality control of I. tectorum.

Objectives:To establish hybridomas secreting monoclonal antibodies(McAbs) against O6-methylguanine-DNA methyltransferase(MGMT) and to observe the relationship between MGMT expression and clinical responses to ACNU and BCNU in human brain tumors.Methods:The hybridomas were established by cell fusion.MGMT expression in 60 glioma specimens was detected by means of immunohistochemical assay.Results: Seven hybridomas secreting McAbs against MGMT were obtained.Thirty tumor specimens had no detectable or low level of MGMT expression(Mer-), while 30 specimens had high level of MGMT expression(Mer+). The Mer- patients showed more sensitive to ACNU and BCNU than the Mer+ patients.Conclusions: The high specific hybridomas secreting monoclonal antibodies(McAbs) against MGMT were established.The preliminary study indicated that MGMT negative tumors were sensitive to ACNU and BCNU, whereas MGMT positive ones were more resistant to nitrosourea drugs.