Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Jerome J. Jendrisak"'
Publikováno v:
Analytical Biochemistry. 79:181-189
Three artefacts have been identified which can reverse the preference of wheat germ RNA Polymerase II for native over heat-denatured calf thymus DNA. Self-absorption during liquid scintillation counting, contamination of DNA with RNase, and the use o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4784e2e69091972859f095514d94640d
https://doi.org/10.1016/0003-2697(77)90392-x
https://doi.org/10.1016/0003-2697(77)90392-x
Publikováno v:
Biochemistry. 14:4639-4645
An improved method for the purification of the alpha-amanitin-sensitive deoxyribonucleic acid dependent ribonucleic acid polymerase [ribonucleosidetriphosphate:RNA-nucleotidyltransferase, EC 2.7.7.6-A1 (RNA polymerase II or RNA polymerase B) from whe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abd86dd8986c37ffd51c47ae259edb77
https://doi.org/10.1021/bi00692a012
https://doi.org/10.1021/bi00692a012
Autor:
Jerome J. Jendrisak, Wayne M. Becker
Publikováno v:
Biochemical Journal. 139:771-777
A procedure is described for the purification of the α-amanitin-sensitive DNA-dependent RNA polymerase [EC 2.7.7.6] from wheat germ. Solubilization of the enzyme activity was achieved by sonication of a crude extract in a high-salt buffer. Purificat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64448cc18a9a1969e3d04a7e7e609c8a
https://doi.org/10.1042/bj1390771
https://doi.org/10.1042/bj1390771
Publikováno v:
Journal of Biological Chemistry. 256:5860-5865
Wheat germ contains an enzyme capable of removing supercoils from circular DNA. We have purified this enzyme using Polymin P fractionation, ammonium sulfate precipitation, and chromatography on Bio-Rex 70 and phenyl-Sepharose. Renaturation after elec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7a1ad0fec42850c27d4a451afa9cfac3
https://doi.org/10.1016/s0021-9258(19)69287-2
https://doi.org/10.1016/s0021-9258(19)69287-2
Publikováno v:
Plant physiology. 54(3)
Two DNA-dependent RNA polymerases (ribonucleoside triphosphate:RNA nucleotidyl transferase, EC 2.7.7.6) have been isolated from pea (Pisum sativum) seedlings. The enzymes were solubilized by sonication in high salt buffer and were separated by chroma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e7e36d1472ad06636079ac667e5574e
https://pubmed.ncbi.nlm.nih.gov/16658887
https://pubmed.ncbi.nlm.nih.gov/16658887
Publikováno v:
Biochemistry. 16(9)
We have previously presented a rapid, high yield method for the large scale purification of homogeneous RNA polymerase II from wheat germ (Jendrisak, J.J., and Burgess, R.R.(1975), Biochemistry 14, 4639), and we now report a detailed study of its sub
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdd640284a3d4fbc12d68dcaff8dd6e6
https://pubmed.ncbi.nlm.nih.gov/857883
https://pubmed.ncbi.nlm.nih.gov/857883
Publikováno v:
Biochemistry. 14(21)
An improved method is described for the purification of the DNA-dependent RNA polymerase [ribonucleosidetriphosphate:RNA nucleotidyltransferase, EC 2.7.7.6] from Escherichia coli. The method involves lysozyme-sodium deoxycholate lysis, low-speed cent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86e5a7fe07807dbab6552e7c3a68bf08
https://pubmed.ncbi.nlm.nih.gov/1101952
https://pubmed.ncbi.nlm.nih.gov/1101952
Publikováno v:
Biochemical and biophysical research communications. 74(3)
Atomic absorption studies indicate that the DNA-dependent RNA polymerase II from wheat germ contains about 7 tightly bound zinc atoms per enzyme molecule. This value has been repeatedly obtained with a number of enzyme preparations subjected to varyi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d91acc9356738ecc96b61f756997b09
https://pubmed.ncbi.nlm.nih.gov/843344
https://pubmed.ncbi.nlm.nih.gov/843344
Autor:
Jerome J. Jendrisak, Wayne M. Becker
Publikováno v:
Biochimica et biophysica acta. 319(1)
Two DNA-dependent RNA polymerases (ribonucleoside triphosphate: RNA nucleotidyltransferase, EC 2.7.7.6) have been isolated from wheat germ. The enzymes were solubilized by high salt extraction with sonication and were resolved by DEAE-cellulose chrom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7332e9063822eced7d99015b29415148
https://pubmed.ncbi.nlm.nih.gov/4739046
https://pubmed.ncbi.nlm.nih.gov/4739046