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Application
Cellulose phosphate is used in protein chromatography, ion exchange chromatography and cation exchange media. Cellulose phosphate (CELLPHOS) has been studied as a collector for analytical preconcentration of traces of Cd(II), Cr(III), Cu(II) and Ni(II) from aqueous sample solution and used to purify and characterize acid phosphatase from approximately 3000-year-old human bones from archeological excavations.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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[Isolation and purification of nonspecific nuclease of cyanobacterium Plectonema boryanum CALU 465].
Mikrobiolohichnyi zhurnal (Kiev, Ukraine : 1993), 66(1), 29-35 (2004-04-24)
Nonspecific nuclease has been isolated from the cells of cyanobacterium Plectonema boryanum and purified to homogenic state. It has been established that the method of centrifugation of cell-free culture extract in the sucrose density gradient is efficient for the separation
Preparative biochemistry & biotechnology, 33(4), 311-320 (2003-11-11)
In this research, acid phosphatase was purified and characterized from approximately 3000-year-old human bones from archeological excavations. Using anion exchange chromatography, two isoenzymes, TrACP and TsACP, were isolated from the bone. TrACP and TsACP were eluted separately, with a concentration
Current protocols in molecular biology, Chapter 18, Unit 18-Unit 18 (2008-02-12)
In studies of the regulation of specific biochemical events by reversible phosphorylation, assaying the protein kinases themselves can often lead to significant progress in understanding the mechanistic details of a system under study. This unit describes assays for a variety
Overexpression and purification of Saccharomyces cerevisiae DNA topoisomerase II from yeast.
Methods in molecular biology (Clifton, N.J.), 94, 187-197 (2003-07-08)
Biochemistry, 41(16), 5255-5265 (2002-04-17)
Plasmid DNA replication in nuclear extracts of Saccharomyces cerevisiae in vitro has been shown to be S-phase specific, similar to that observed in vivo. We report here a reconstituted in vitro system with partially purified replication proteins, purified replication protein
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