Id |
Subject |
Object |
Predicate |
Lexical cue |
TextSentencer_T1 |
0-112 |
Sentence |
denotes |
Purification and characterization of avian beta 1,4 galactosyltransferase: comparison with the mammalian enzyme. |
T1 |
0-112 |
Sentence |
denotes |
Purification and characterization of avian beta 1,4 galactosyltransferase: comparison with the mammalian enzyme. |
T1 |
0-112 |
Sentence |
denotes |
Purification and characterization of avian beta 1,4 galactosyltransferase: comparison with the mammalian enzyme. |
TextSentencer_T2 |
113-345 |
Sentence |
denotes |
Avian beta 1,4 galactosyltransferase (GalTase) was purified from chicken serum, partially characterized and compared to mammalian GalTase using antibody cross-reactivity, Northern blot hybridization and amino acid sequence analysis. |
T2 |
113-345 |
Sentence |
denotes |
Avian beta 1,4 galactosyltransferase (GalTase) was purified from chicken serum, partially characterized and compared to mammalian GalTase using antibody cross-reactivity, Northern blot hybridization and amino acid sequence analysis. |
T2 |
113-345 |
Sentence |
denotes |
Avian beta 1,4 galactosyltransferase (GalTase) was purified from chicken serum, partially characterized and compared to mammalian GalTase using antibody cross-reactivity, Northern blot hybridization and amino acid sequence analysis. |
TextSentencer_T3 |
346-591 |
Sentence |
denotes |
The enzyme was purified to apparent homogeneity by alpha-lactalbumin(LA)-agarose affinity chromatography followed by preparative SDS-polyacrylamide gel electrophoresis, and identified as two proteins of apparent molecular masses of 39 and 46 kD. |
T3 |
346-591 |
Sentence |
denotes |
The enzyme was purified to apparent homogeneity by alpha-lactalbumin(LA)-agarose affinity chromatography followed by preparative SDS-polyacrylamide gel electrophoresis, and identified as two proteins of apparent molecular masses of 39 and 46 kD. |
T3 |
346-591 |
Sentence |
denotes |
The enzyme was purified to apparent homogeneity by alpha-lactalbumin(LA)-agarose affinity chromatography followed by preparative SDS-polyacrylamide gel electrophoresis, and identified as two proteins of apparent molecular masses of 39 and 46 kD. |
TextSentencer_T4 |
592-727 |
Sentence |
denotes |
Chicken serum GalTase had a Km for UDPGal of 42 microM, for GlcNAc of 10 mM and had optimal activity in the presence of 10-20 mM MnCl2. |
T4 |
592-727 |
Sentence |
denotes |
Chicken serum GalTase had a Km for UDPGal of 42 microM, for GlcNAc of 10 mM and had optimal activity in the presence of 10-20 mM MnCl2. |
T4 |
592-727 |
Sentence |
denotes |
Chicken serum GalTase had a Km for UDPGal of 42 microM, for GlcNAc of 10 mM and had optimal activity in the presence of 10-20 mM MnCl2. |
TextSentencer_T5 |
728-1150 |
Sentence |
denotes |
Substrate and linkage specificity analyses indicated that the purified enzyme behaves as a traditional Gal beta 1,4 GlcNAc:GalTase, since: (i) the avian beta 1,4 GalTase bound to alpha-LA; (ii) terminal GlcNAc residues served as good acceptors for chicken serum GalTase; (iii) the enzyme was inhibited by high concentrations of GlcNAc; (iv) the galactosylated product was sensitive to beta 1,4-specific beta-galactosidase. |
T5 |
728-1150 |
Sentence |
denotes |
Substrate and linkage specificity analyses indicated that the purified enzyme behaves as a traditional Gal beta 1,4 GlcNAc:GalTase, since: (i) the avian beta 1,4 GalTase bound to alpha-LA; (ii) terminal GlcNAc residues served as good acceptors for chicken serum GalTase; (iii) the enzyme was inhibited by high concentrations of GlcNAc; (iv) the galactosylated product was sensitive to beta 1,4-specific beta-galactosidase. |
T5 |
728-1150 |
Sentence |
denotes |
Substrate and linkage specificity analyses indicated that the purified enzyme behaves as a traditional Gal beta 1,4 GlcNAc:GalTase, since: (i) the avian beta 1,4 GalTase bound to alpha-LA; (ii) terminal GlcNAc residues served as good acceptors for chicken serum GalTase; (iii) the enzyme was inhibited by high concentrations of GlcNAc; (iv) the galactosylated product was sensitive to beta 1,4-specific beta-galactosidase. |
TextSentencer_T6 |
1151-1258 |
Sentence |
denotes |
Finally, the disaccharide reaction product comigrated with authentic beta 1,4 N-acetyllactosamine standard. |
T6 |
1151-1258 |
Sentence |
denotes |
Finally, the disaccharide reaction product comigrated with authentic beta 1,4 N-acetyllactosamine standard. |
T6 |
1151-1258 |
Sentence |
denotes |
Finally, the disaccharide reaction product comigrated with authentic beta 1,4 N-acetyllactosamine standard. |
TextSentencer_T7 |
1259-1351 |
Sentence |
denotes |
No other GalTase activities were detectable using a battery of defined glycoside substrates. |
T7 |
1259-1351 |
Sentence |
denotes |
No other GalTase activities were detectable using a battery of defined glycoside substrates. |
T7 |
1259-1351 |
Sentence |
denotes |
No other GalTase activities were detectable using a battery of defined glycoside substrates. |
TextSentencer_T8 |
1352-1504 |
Sentence |
denotes |
Polyclonal antibodies raised against the two gel-purified GalTase proteins showed reactivity with avian GalTase by ELISA and immunoprecipitation assays. |
T8 |
1352-1504 |
Sentence |
denotes |
Polyclonal antibodies raised against the two gel-purified GalTase proteins showed reactivity with avian GalTase by ELISA and immunoprecipitation assays. |
T8 |
1352-1504 |
Sentence |
denotes |
Polyclonal antibodies raised against the two gel-purified GalTase proteins showed reactivity with avian GalTase by ELISA and immunoprecipitation assays. |
TextSentencer_T9 |
1505-1616 |
Sentence |
denotes |
The antibodies also inhibited GalTase activity toward both high mol. wt and monosaccharide acceptor substrates. |
T9 |
1505-1616 |
Sentence |
denotes |
The antibodies also inhibited GalTase activity toward both high mol. wt and monosaccharide acceptor substrates. |
T9 |
1505-1616 |
Sentence |
denotes |
The antibodies also inhibited GalTase activity toward both high mol. wt and monosaccharide acceptor substrates. |
TextSentencer_T10 |
1617-1933 |
Sentence |
denotes |
Despite similar kinetics and substrate specificity, the avian and mammalian GalTases showed little overall structural similarity, since polyclonal anti-avian GalTase IgG failed to react with mammalian GalTase purified from bovine milk, and conversely anti-bovine milk GalTase IgG did not react with the avian enzyme. |
T10 |
1617-1933 |
Sentence |
denotes |
Despite similar kinetics and substrate specificity, the avian and mammalian GalTases showed little overall structural similarity, since polyclonal anti-avian GalTase IgG failed to react with mammalian GalTase purified from bovine milk, and conversely anti-bovine milk GalTase IgG did not react with the avian enzyme. |
T10 |
1617-1933 |
Sentence |
denotes |
Despite similar kinetics and substrate specificity, the avian and mammalian GalTases showed little overall structural similarity, since polyclonal anti-avian GalTase IgG failed to react with mammalian GalTase purified from bovine milk, and conversely anti-bovine milk GalTase IgG did not react with the avian enzyme. |
TextSentencer_T11 |
1934-2125 |
Sentence |
denotes |
Furthermore, in Northern blot analysis, no hybridization was detected when chicken embryo liver poly(A)+ RNA was probed with a mouse GalTase cDNA, even under conditions of reduced stringency. |
T11 |
1934-2125 |
Sentence |
denotes |
Furthermore, in Northern blot analysis, no hybridization was detected when chicken embryo liver poly(A)+ RNA was probed with a mouse GalTase cDNA, even under conditions of reduced stringency. |
T11 |
1934-2125 |
Sentence |
denotes |
Furthermore, in Northern blot analysis, no hybridization was detected when chicken embryo liver poly(A)+ RNA was probed with a mouse GalTase cDNA, even under conditions of reduced stringency. |
TextSentencer_T12 |
2126-2332 |
Sentence |
denotes |
Amino acid sequence analysis identified three of five tryptic peptides that are homologous to the mammalian sequence within a putative substrate binding domain and the carboxy terminal domain of the enzyme. |
T12 |
2126-2332 |
Sentence |
denotes |
Amino acid sequence analysis identified three of five tryptic peptides that are homologous to the mammalian sequence within a putative substrate binding domain and the carboxy terminal domain of the enzyme. |
T12 |
2126-2332 |
Sentence |
denotes |
Amino acid sequence analysis identified three of five tryptic peptides that are homologous to the mammalian sequence within a putative substrate binding domain and the carboxy terminal domain of the enzyme. |
TextSentencer_T13 |
2333-2495 |
Sentence |
denotes |
Their overall structural disparity leads us to believe that regions of homology between the avian and mammalian GalTases may represent active sites of the enzyme. |
T13 |
2333-2495 |
Sentence |
denotes |
Their overall structural disparity leads us to believe that regions of homology between the avian and mammalian GalTases may represent active sites of the enzyme. |
T13 |
2333-2495 |
Sentence |
denotes |
Their overall structural disparity leads us to believe that regions of homology between the avian and mammalian GalTases may represent active sites of the enzyme. |