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1

Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei

100%
Kruszewska J. S., Perlinska-Lenart U., Palamarczyk G.
Acta Biochimica Polonica
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1996
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tom 43
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nr 2
Mannosylphosphodolichol synthase (MPD-synthase) (EC 2.4.1.830) catalyzing formation of MPD from GDPMan and dolichylphosphate (PD) has been purified from T. reesei cellular membranes almost to homogeneity. Selective solubilization of the enzyme was followed by one step purification on Phenyl-Sepharose column. SDS/ PAGE of the purified enzyme fraction revealed the presence of a protein band of 31 kDa corresponding to the apparent molecular mass of the MPD-synthase purified from S. cerevisiae [Babczinski, P. et al. (1980) Eur. J. Biochem. 105,509-515; Haselbeck A. (1989) Eur. /. Biochem. 181, 663-6681. During solubilization, the enzyme was stabilized by the presence of a lipophilic substrate dolichylphosphate and phospholipids as well as by protease inhibitors. The Phenyl-Sepharose purified enzyme had an absolute requirement for dolichylphosphate and was activated by cAMP dependent protein kinase.
2
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Enhanced production, purification and characterization of alkaline keratinase from Streptomyces minutiscleroticus DNA38

86%
Allure N., D.N. M., Agsar D.
International Letters of Natural Sciences
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2015
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tom 43
A thermo tolerant, feather-degrading, newly isolated actinobacterial strain Streptomyces minutiscleroticus DNA38 was investigated for its ability to produce keratinase. Maximum production (283.4 IU) of keratinase by Streptomyces minutiscleroticus DNA38 in starch chicken feathers medium under submerged bioprocess was observed at optimized conditions of pH 9.0 of the medium and 45 °C incubation temperature. Further, an enhanced production (435.8 IU) of keratinase was achieved employing response surface methodology. Combined interactive effect of starch (7.50 g/L), yeast extract (0.74 g/L) and chicken feathers (7.50 g/L) were found to be the critical process variables for enhanced production under central composite design. Chicken feathers showed a direct action and addition of starch and yeast extract to the medium proved effective for a significant increase in the production of keratinase. The purified keratinase was monomeric and had a molecular mass of 29 kDa. The enzyme activity was significantly inhibited after pH 9.0 and temperature 50 °C.
3

Partial purification and characterization of L-myo-inositol-1-phosphate synthase of pteridophytic origin

86%
Chhetri D. R., Mukherjee A. K., Adhikari J.
Acta Physiologiae Plantarum
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2006
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tom 28
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nr 2
Myo-Inositol is an important metabolite for normal growth and development of all living organisms. The cellular level of myo-inositol is con-rolled by the enzyme L-myo- inositol-1-phosphate synthase (MIPS) [EC 5.5.1.4]. Appreciable level of MIPS activity was detected from the common pteridophytes like Dicranopteris, Diplazium, Diplopterygium, Equisetum, Lycopodium, Polypodium, Pteridium, Selaginella etc. available in Darjeeling Himalayas. The enzyme was partially purified from the reproduc-ive pinnules of Diplopterygium glaucum (Thunb.) Nakai. The purification obtained was about 81 fold and the recovery was about 13.5 %. The final enzyme preparation specifically utilized D-Glucose-6-phosphte and NAD+ as its substrate and co-factor respectively. It shows pH optima between 7.0 and 7.5 while the temperature maximum was at 35 °C. The enzyme activity was slightly inhibited by Na+ and Cd2+ and highly inhibited by Li+ and Hg2+. The Krn values for D-glucose-6-phosphate and NAD+ was found to be as 0.83 mM and 0.44 mM respectively while the Vmax values were 1.42 mM and 1.8 mM for D-glucose-6-phosphate and NAD+ respectively. The present study indicates the universal occurrence of this enzyme in all plant groups.
4

Isolation and characterization of pigeon breast muscle cytosolic 5'-nucleotidase-I [cN-I]

86%
Tkacz-Stachowska K., Lechward K., Skladanowski A. C.
Acta Biochimica Polonica
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2005
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tom 52
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nr 4
5´-Nucleotidase specific towards dCMP and AMP was isolated from avian breast muscle and characterized. It was found to be similar to a type-I form (cN-I) identified earlier as the AMP-selective 5´-nucleotidase responsible for adenosine formation during ATP breakdown in transfected COS-7 cells. Expression pattern of the cN-I gene in pigeon tissues indicated breast muscle as a rich source of the transcript. We purified the enzyme from this source using two-step chromatography and obtained an active homogenous preparation, free of ecto-5´-nucleotidase activity. The tissue content of the activity was calculated at 0.09 U/g wet weight. The specific activity of the enzyme preparation was 4.33 U/mg protein and it preferred dCMP and AMP to dAMP and IMP as a substrate. Its kinetic properties were very similar to those of the enzyme purified earlier from heart tissue. It was strongly activated by ADP. Inhibition by inorganic phosphate was more pronounced than in heart-isolated cN-I. Despite this difference, a similar physiological function is suggested for cN-I in both types of muscle.
5

Properties of trehalase from different organs of alfalfa, Medicago sativa

58%
Wolska-Mitaszko B., Molestak E., Malek W.
Acta Physiologiae Plantarum
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2005
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tom 27
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nr 1
Trehalase activity (THA) was identified in the cell-free extracts of various organs of Medicago sativa: roots, roots nodules, stems and leaves, as well as in seediings and seeds. It showed the high activity at acid pH and optimal temperature ranged from 45 ℃ to 55 °C. It was also differently affected by ions, i.e. the presence of calcium stimulated this activity but it was inhibited by Zn2+ and NH4+. After separation by DEAE-cellulose chromatography and purification procedures, trehalase from alfalfa was purified 800 times, and Superose 12 HR gel filtration allowed to determine the molecular weight of 120 kDa for the native enzyme from the stems of alfalfa.
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