Purification and characterization of UDP-GalNAc:polypeptide N-acetylgalactosamine transferase from an ascites hepatoma, AH 66.
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UDP-N-Acetylgalactosamine: globoside a-3-N-Acetylgalactos- aminyltransferase
A UDP-N-acetylgalactosamine:globoside a-3-N-acetylgalactosaminyltransferase has been purified over 3500-fold in 4% yield from a Triton X-100 extract of canine spleen microsomes by affinity chromatography on globoside acid-agarose. Sodium dodecyl sulfate gel electrophoresis of the purified enzyme revealed two major bands with molecular weights of 66,000 and 56,000. Judging from the molecular wei...
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Partial purification of a thioredoxin system from Novikoff ascites hepatoma cells has been previously reported (MOORE, E. C. (1967) Biochem. Biophys. Res. Commun. 29, 264-268). Thioredoxin from the same mammalian source has now been purified to electrophoretic homogeneity by ammonium sulfate fractionation, heat treatment, DEAE-cellulose chromatography, and Sephadex chromatography. 1-Dimethylami...
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A UDP-N-acetylgalactosamine:globotriaosylceramide beta-3-N-acetylgalactosaminyltransferase which catalyzes the conversion of human blood group Pk antigen into P antigen has been purified over 18,000-fold in 4% yield from a Triton X-100 extract of canine spleen microsomes by affinity chromatography on UDP-hexanolamine-Sepharose and globotriaosylceramide acid-Sepharose. The purified enzyme migrat...
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The mitochondria isolated in isotonic sucrose from AH-130 Yoshida ascites hepatoma appear spontaneously swollen (11, 12). This spontaneous swelling may be in part responsible for the inability of tumor mitochondria to undergo extensive volume changes in hypotonie conditions or in conditions that induce large-amplitude, metabolic-dependent, or metabolic-independent swelling in normal liver mitoc...
متن کاملEhrlich Ascites Tumor Cell UDP - Ga 1 : N - Acetyl - D - glucosamine , 8 ( 1 , 4 ) - Galactosyltransferase PURIFICATION
A UDP-Ga1:N-acetylglucosamine B( l,l)-galactosyltransferase which catalyzes the synthesis of 8-DGal( l,l)-~-GlcNAc units has been purified 17,560-fold from Ehrlich tumor cells to apparent electrophoretic homogeneity. The enzyme appears to be a monomeric protein with M, = 56,000-58,000. Enzymatic activity requires the presence of MnC12, is stimulated by detergent, and exhibits a pH optimum at 6...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1982
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)34098-5