Purification and characterization of archaeal 6xHis tagged recombinant proteases

Date

2006-06-01

Author

Koyuncu, B.
Demirok, B.
Kocabıyık, Semra

Metadata

Show full item record

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

Item Usage Stats

98
views

0
downloads

URI

https://hdl.handle.net/11511/53326

Collections

Department of Biology, Conference / Seminar

Suggestions

OpenMETU
Core

Purification and characterization of cytoplasmic and proteasome associated chymotrypsin-like proteases from Thermoplasma volcanium Özdemir, F. İnci; Kocabıyık, Semra; Department of Biology (2003) In this study, two novel cytoplasmic serine proteases were isolated and characterized from thermophilic archaea Thermoplasma volcanium. The first protease was purified by ion exchange and affinity chromatographies and identified as a chymotrypsin-like serine protease mainly based on its substrate profile and inhibition pattern. The presence of protease activity was analyzed by gelatin zymography which was detected as a single band (35 kDa). Optimum temperature was found to be 60oC for azocasein hydrolysis a...
Purification and characterization of Hexokinase isoenzymes from Rhizopus oryzae Dedeoğlu, Didem; Hamamcı, Haluk; Department of Biotechnology (2007) Glycolysis is the central metabolic pathway for living organisms. Its regulation is important for the yield of the end products which are industrially important. These end products, like lactic acid produced by Rhizopus oryzae, are industrially important. Rhizopus oryzae is a filamentous fungus producing lactic acid and ethanol. The lactic acid yield of R. oryzae is low (70 %) compared to that of lactic acid bacteria (95 %) still it is noteworthy because R. oryzae produces only the L (+) form of lactic acid...
Purification and characterization of cytocchrome b5 from sheep liver microsomes Yalçın, Deniz; Arınç Emel; Department of Biochemistry (1998)
Purification and Characterization of Cytochrome P450 Reductase from Liver Microsomes of Feral Leaping Mullet (Liza saliens) Sen, Alaattin; Arinc, Emel (Wiley, 1998-01-01) NADPH-cytochrome P450 reductase was purified to electrophoretic homogeneity from detergent-solubilized liver microsomes from the leaping mullet (Liza saliens). The purified reductase was characterized with respect to spectral, electrophoretic, and biocatalytic properties. In addition, effects of pH, ionic strength, and the substrate concentration on the NADPH-dependent cytochrome c reductase activity of the purified fish liver cytochrome P450 reductase were studied. Cytochrome P450 reductase was purified 43...
Purification, characterization and identification of a novel bifunctional catalase-phenol oxidase from Scytalidium thermophilum Kocabas, D. Sutay; Bakir, U.; Phillips, S. E.; Mcpherson, M. J.; Ögel, Zümrüt Begüm (2009-09-01)

Citation Formats

B. Koyuncu, B. Demirok, and S. Kocabıyık, “Purification and characterization of archaeal 6xHis tagged recombinant proteases,” 2006, vol. 273, Accessed: 00, 2020. [Online]. Available: https://hdl.handle.net/11511/53326.