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Sudha Rao Gopalakrishna Kamath Gururaj Maralihalli Anil S. Bhagwat 《Photosynthesis research》1987,12(2):155-164
The -aminolevulinic acid dehydratase activity was irreversibly inactivated by irradiation of the enzyme in presence of flavin mononucleotide. The loss of enzyme activity was dependent on time of irradiation, concentration of FMN and intensity of irradiance. It required oxygen and was markedly enhanced in heavy water. The presence of levulinic acid (a competitive inhibitor of -ALAD) during irradiation prevented the inactivation considerably indicating photooxidative damage at or near the active site. Superoxide dismutase, sodium benzoate and sodium formate offered no protection, but singlet oxygen quenchers like azide and tryptophan were effective. NADH, electron donor to excited flavins, also prevented the loss of enzyme activity. These results indicate that singlet oxygen produced by light absorption of FMN was responsible for the photooxidative inhibition of the enzyme.Abbreviations ALAD
-aminolevulinic acid dehydratase
- FMN
flavin mononucleotide
- O2
-
superoxide
- H2O2
hydrogen peroxide
- 102
singlet oxygen
- LA
levulinic acid
- PBG
porphobilinogen
- BSA
bovine serum albumin
- BME
2-mercaptoethanol
- SOD
superoxide dismutase
- pHMB
para-hydroxymercuribenzoate
- DTT
dithiothreitol
- FAD
flavin adenine dinucleotide
- NADH
nicotinamide adenine dinucleotide 相似文献
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Plasminogen activator secreted by lymphosarcoma (ascites) of mice was purified up to 163-fold by ammonium sulphate fractionation
at 35% saturation and chromatography on p-aminobenzamidine-Sepharose 4B. The purified activator contained specific activity
of 9980 IU/mg. The plasminogen activator displayed homogeneity by polyacrylamide slab gel electrophoresis and high performance
liquid chromatography. The activator consisted of a single polypeptide chain with an apparent molecular weight of 66,000 daltons
as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis under reducing conditions as well as gel filtration
on Sephadex G-100. Distinct differences between this activator and urokinase were discernible in respect of specific activities,
fibrin affinity and immunochemical properties. The lymphosarcoma activator appears to be of tissue-type origin since it showed
gross similarity to standard tissue plasminogen activator in terms of modes of binding to fibrin and immunological attributes. 相似文献
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Sreedhara Sangadala Subramanian Sivakami Joseph Mendicino 《Molecular and cellular biochemistry》1991,101(2):125-143
Summary Two specific -N-acetylglucosaminyltransferases involved in the branching and elongation of mucin oligosaccharide chains, namely, a 1,6 N-acetylglucosaminylsaminyltransferase that transfers N-acetylglucosamine from UDP-N-acetylglucosamine to Gal3GalNAc-Mucin to yield Gal3(GlcNAc6)GalNAc-Mucin and a 3-N-acetylglucosaminyl transferase that transfers N-acetylglucosamine from UDP-N-acetylglucosamine to Gal3(GlcNAC6)GalNAc-mucin to yield GlcNAc3Gal3 (GlcNAc6)GalNAc-Mucin were purified from the microsomal fraction of swine trachea epithelium. The 1,6-N-acetylglucosaminyltransferase was purified about 21,800-fold by procedures which included affinity chromatography on DEAE columns containing bound asialo Cowper's gland mucin glycoprotein with Gal1,3GalNAc side chains. The apparent molecular weight estimated by gel filtration was found to be about 60 Kd. The purified enzyme showed a high specificity for Gal1,3GalNAc chains and the most active substrates were mucin glycoproteins containing these chains. The apparent Km of the 6-glucosaminyltrans-ferase for Cowper's gland mucin glycoprotein containing Gal1,3GalNAc chains was 0.53 µM; for UDP-N-acetylglucosamine, 12 µM; and for Gal 1,3GalNAc NO2ø, 4 mM. The activity of the 6-glucosaminyltransferase was dependent on the extent of glycosylation of the Gal3GalNAc chains in Cowper's gland mucin glycoprotein.The best substrate for the partially purified 3-Glucosaminyltransferase was Cowper's gland mucin glycoprotein containing Gal1,3(GlcNAc6)GalNAc side chains. This enzyme showed little or no activity with intact sialylated Cowper's gland mucin glycoprotein or derivatives of this glycoprotein containing GalNAc or Gal1,3GalNAc side chains.The radioactive oligosaccharides formed by these enzymes in large scale reaction mixtures were released from the mucin glycoproteins by treatment with alkaline borohydride, isolated by gel filtration on Bio-Gel P-6 and characterized by methylation analysis and sequential digestion with exoglycosidases. The oligosaccharide products formed by the 6- and 3-glucosaminyltransferases were shown to be Gal3(GlcNAC6) GalNAc and GlcNAc3 Gal3(GlcNAC6)GalNAc respectively.Taken collectively, these results demonstrate that swine trachea epithelium contains two specific N-acetylglucosaminyltransferases which catalyze the initial branching and elongation reactions involved in the synthesis of O-linked oligosaccharide chains in respiratory mucin glycoproteins. The first enzyme a 6-glucosaminyltransferase converts Gal3GalNAc chains in mucin glycoproteins to Gal3(GlcNAc6)GalNAc chains. This product is the substrate for a second 3-glucosaminyltransferase which converts the Gal3(GlcNAc6)GalNAc chains to GlcNAc3Gal(GlcNAc6)GalNAc chains in the glycoprotein. The 3-glucosaminyltransferase did not utilize Gal3GalNAc chains as a substrate and this results in an ordered sequence of addition of N-acetylglucosamine residues to growing oligosaccharide chains in tracheal mucin glycoproteins.Abbreviations NeuNAc
N-acetylneuraminic acid
- GalNAcol
N-acetylgalactosaminitol
- CGMG
Cowper's gland mucin glycoprotein
- GalNAc-CGMG
Cowper's gland mucin glycoprotein containing GalNAc side chains O-glycosidically linked to serine or threonine
- Gal3GalNAc-CGMC
Cowper's gland mucin glycoprotein containing Gal3GalNAc side chains
- MES
2-(N-morpholino) Ethane Sulfonic acid
- PBS
Phosphate Buffered Saline 相似文献