The conversion of group B red blood cells into group O by an α-d-galactosidase from taro (Colocasia esculenta)

Chien, Su-Fang; Lin‐Chu, M.

doi:10.1016/0008-6215(91)84129-3

Cited by 11 publications

(9 citation statements)

References 18 publications

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“…Furthermore, there was a commercial application of the enzyme as a supplement in animal feed to increase animal meat production. Finally, rice α-galactosidase may be useful for blood conversion purpose (Harpaz et al 1977;Lenny et al 1994;Zarnitz and Kabat 1960;Zhu et al 1995) since its ability to convert blood type is comparable with that of the taro enzyme (Chien 1991). In fact, we were the first to show that the rice α-galactosidase was capable to convert B red blood cells into O red cells.…”

Section: Discussionmentioning

confidence: 91%

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Cloning, Expression, and Characterization of Rice α-Galactosidase

2008

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We have successfully cloned an α-galactosidase gene from a rice cDNA library and transformed it into Escherichia coli BL21. It was subsequently cloned to the pPIC9K vector and expressed in Pichia pastoris. A selected clone was found to result in high production yield of the galactosidase enzyme. The secreted enzyme was purified, and it revealed as a major protein band on an SDS-PAGE gel. The optimal pH value, enzyme stabilities, and substrate specificity were studied. The enzyme specificity toward the terminal α1→6, 1→4, and 1→3 linked galactosyl residue from various substrates was investigated. By determining the Michelis constant (Km) of the enzyme for melibiose, raffinose, and stachyose, our results showed that melibiose was hydrolyzed faster than raffinose, whereas the published data reported a reversed sequence, raffinose > melibiose. The enzyme also showed the ability of converting B red blood cells into O red cells. The objective of this work is to develop the Pichia system to produce a large quantity of enzyme for blood cell conversion for transfusion.

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Section: Discussionmentioning

confidence: 91%

“…Hemagglutination procedure was carried out at different time periods by adding 15 μl of anti-B or anti-H (Goldstein and Poretz 1986) to 20 μl of the reaction mixture. Agglutination was carried out according to the procedure established in our lab (Chien 1991).…”

Section: B Red Blood Cells Conversion Into O Red Cellsmentioning

confidence: 99%

Cloning, Expression, and Characterization of Rice α-Galactosidase

2008

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“…In theory, group O RBCs could be created from cells of another ABO blood group if the A and B terminal sugars (between 120,000 and 1,170,000 sites/cell for A, and 610,000‐830,000 sites/cell for B 6 ) could be removed. Many naturally occurring exogly‐cosidases purified from plants and microorganisms can accomplish this task 7–12 . The resulting cells, while of interest for in vitro research, have not been considered suitable for clinical transfusion purposes.…”

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confidence: 99%

Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O

et al. 2000

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“…The rice α-galactosidase gene was isolated from the stem portion of taro (Colocasia esculenta) that has been demonstrated to have the capability of converting group B into group O red blood cells [7]. In this paper, we describe the use of oligonucleotide-loaded nanoparticles to enhance the expression of rice α-galactosidase gene in yeast cells.…”

Section: Introductionmentioning

confidence: 99%

Nanomaterials Enhanced Gene Expression in Yeast Cells

Chien

Chen

Lin

2008

Journal of Nanomaterials

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Metal nanomaterials are shown to enhance gene expression for rice -galactosidase gene (-Gal) in yeast cells. Au and Ag nanoparticles and their nanocomposites, silica-Au and silica-Ag, were prepared and characterized by UV-vis spectroscopy and TEM technique. The rice -galactosidase gene was cloned into the yeast chromosome, where the cloned cells were precultured and induced into a medium containing each of the testing nanomaterials. The nanomaterials were observed to incorporate inside the cells, and no cell death has been detected during the course of gene expression. The enzyme activity was determined by a synthetic substrate, p-nitrophenyl--D-galctopyranoside, and the yellow product yield was recorded in a spectrophotometer at 400 nm. When Au and Ag nanoparticles were incorporated with the culture, a 3–5 fold enhancement in -galactosidase was observed for intracellular activity as well as the secreted activity into the medium. The secreted protein was analyzed to have a pure form and displayed as a single protein band in the SDS-gel electrophoresis. The effects of size and chemical nature of nanomaterials on gene expression for the rice -galactosidase gene in yeast cells are discussed.

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The conversion of group B red blood cells into group O by an α-d-galactosidase from taro (Colocasia esculenta)

Cited by 11 publications

References 18 publications

Cloning, Expression, and Characterization of Rice α-Galactosidase

Cloning, Expression, and Characterization of Rice α-Galactosidase

Transfusion to blood group A and O patients of group B RBCs that have been enzymatically converted to group O

Nanomaterials Enhanced Gene Expression in Yeast Cells

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