Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Moonmoon, Mitra"'
Autor:
Hsin-Yeh, Hsieh, Hsieh, Hsin-Yeh, Linda F, Chapman, Michael J, Calcutt, Moonmoon, Mitra, Daniel S, Smith
Publikováno v:
Artificial Cells, Blood Substitutes, and Biotechnology. 33:187-199
The ABO blood group antigens (A, B and H antigens) are composed of complex oligosaccharides linked to membrane proteins and lipids [[1], [2]] and abundant on red blood cell membranes. Each antigen ...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1fdf8c072fc888663ae0b9a6487006e
https://doi.org/10.1081/bio-200055904
https://doi.org/10.1081/bio-200055904
Publikováno v:
IUBMB Life. 50:91-97
Summary® - N -Acetylgalactosaminidasefrom Clostridiumperfringens isanexoglycosidasethatdegradesthehumanbloodtypeAepitope.Ahighlypuri”edpreparationof ® - N -acetylgalactosaminidasewasobtainedfrom C.perfringens bysaltprecipitation,gel”ltration,io
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::077ac6e166d9341138b400428220ffd5
https://doi.org/10.1080/713803702
https://doi.org/10.1080/713803702
Publikováno v:
Biomedicine & Pharmacotherapy. 49:244-250
Summary Conversion of erythrocyte membrane B antigen to H antigen produces blood type O which is universally transfusable. If efficient large-scale production of enzymatically converted red blood cells is to be achieved, then optimal conditions for d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3120cf030106d6f81f36786c388dca17
https://doi.org/10.1016/0753-3322(96)82630-8
https://doi.org/10.1016/0753-3322(96)82630-8
Publikováno v:
Protein expression and purification. 32(2)
Clostridium perfringens alpha-N-acetylgalactosaminidase (alphaNAG) hydrolyzed the terminal N-acetyl-alpha-d-galactosamine from the blood type A(2) antigen producing H antigen, blood type O. Blood type O is universally compatible in the ABO system. Pu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65057b4004155210a87d5ffd7f0b5c60
https://pubmed.ncbi.nlm.nih.gov/14965778
https://pubmed.ncbi.nlm.nih.gov/14965778
Publikováno v:
Clinica chimica acta; international journal of clinical chemistry. 247(1-2)
Soluble antigens, enzyme-linked immunosorbent assays (ELISA), and cell suspension assays were used to study the blood group B activity of Glycine max (soybean) α- d -galactosidase. The enzyme readily hydrolyzed the terminal α- d -galactosyl of the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::120e145902a4cf1bf4a53117b0c5c5d5
https://pubmed.ncbi.nlm.nih.gov/8920223
https://pubmed.ncbi.nlm.nih.gov/8920223
Publikováno v:
Artificial Cells, Blood Substitutes, and Biotechnology. 37:283-283
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::252cd5de2ac110e8ec946e2cbd57bd56
https://doi.org/10.3109/10731190903339061
https://doi.org/10.3109/10731190903339061
Autor:
P. Sun, J Hata, Daniel S. Smith, Michael Harmata, Frederick G. Haibach, Moonmoon Mitra, M Dhar
Publikováno v:
Biochemical and biophysical research communications. 181(3)
Exoglycosidases modify carbohydrate epitopes on glycoproteins and glycolipids. The alpha-D-galactosidase from Coffea canephora is an important exoglycosidase which degrades the human blood group B epitope. Although multiple isozymes have been describ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fbeef4144f076be20342935422e09773
https://pubmed.ncbi.nlm.nih.gov/1662502
https://pubmed.ncbi.nlm.nih.gov/1662502