Show/Hide Menu
Hide/Show Apps
Logout
Türkçe
Türkçe
Search
Search
Login
Login
OpenMETU
OpenMETU
About
About
Open Science Policy
Open Science Policy
Open Access Guideline
Open Access Guideline
Postgraduate Thesis Guideline
Postgraduate Thesis Guideline
Communities & Collections
Communities & Collections
Help
Help
Frequently Asked Questions
Frequently Asked Questions
Guides
Guides
Thesis submission
Thesis submission
MS without thesis term project submission
MS without thesis term project submission
Publication submission with DOI
Publication submission with DOI
Publication submission
Publication submission
Supporting Information
Supporting Information
General Information
General Information
Copyright, Embargo and License
Copyright, Embargo and License
Contact us
Contact us
Purification and Characterization of a Thermostable Serine protease from Thermoplasma volcanium
Date
2001-06-30
Author
Kocabıyık, Semra
Metadata
Show full item record
Item Usage Stats
98
views
0
downloads
Cite This
URI
https://hdl.handle.net/11511/74298
Conference Name
27th Meeting of the Federation of European Biochemical Societies, 2001
Collections
Department of Biology, Conference / Seminar
Suggestions
OpenMETU
Core
Purification and characterization of an intracellular chymotrypsin-like serine protease from Thermoplasma volcanium
Kocabıyık, Semra (2006-01-01)
An intracellular serine protease produced by Thermoplasma (Tp.) voleanium was purified using a combination of ammonium sulfate fractionation, ion exchange, and et-casein agarose affinity chromatography. This enzyme exhibited the highest activity and stability at pH 7.0, and at 50 degrees C. The purifed enzyme hydrolyzed synthetic peptides preferentially at the carboxy terminus of phenylalanine or leucine and was almost completely inhibited by PMSF, TPCK, and chymostatin, similarly to a chymotrypsin-like ser...
Purification and characterization of two fractions of cytochrome b5 from sheep lung
Başaran, Nilay; Arınç, Emel; Adalı, Orhan; Department of Biology (1994)
PURIFICATION AND CHARACTERIZATION OF 2 FORMS OF SOLUBLE NADH CYTOCHROME-B5 REDUCTASES FROM HUMAN ERYTHROCYTES
ARINC, E; Güray, Nülüfer Tülün; SAPLAKOGLU, U; Adalı, Orhan (Elsevier BV, 1992-01-01)
1. Two forms of soluble NADH cytochrome b5 reductase were purified from human erythrocytes. Two distinct fractions both having the NADH cytochrome b5 reductase activity eluted from the second DEAE-cellulose column were further purified by ultrafiltration and 5'-ADP-agarose affinity chromatography.
Purification and characterization of two forms of microsomal cytochrome b5 from sheep lung
Basaran, N; Arinc, E (Elsevier BV, 1998-06-01)
Two forms of cytochrome b5 were purified from detergent solubilized sheep lung microsomes by three successive DEAE-cellulose, Sephadex G-100 and Sephadex G-200 column chromatographies. The specific contents of cytochromes b5-I and b5-II were determined to be 45.4 and 43.8 nmol b5/mg protein, which represented up to 567 and 547-fold purification compared with that of the lung microsomes. The most striking difference between b5-I and b5-II was observed in their elution pattern from the third DEAE-cellulose co...
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
IEEE
ACM
APA
CHICAGO
MLA
BibTeX
S. Kocabıyık, “Purification and Characterization of a Thermostable Serine protease from Thermoplasma volcanium,” presented at the 27th Meeting of the Federation of European Biochemical Societies, 2001, Lisbon, Portekiz, 2001, Accessed: 00, 2021. [Online]. Available: https://hdl.handle.net/11511/74298.