Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Cheryl L. Murray"'
Publikováno v:
Proceedings of the National Academy of Sciences. 78:4912-4916
Initiation factor-independent translation of mRNA derived from bacillus phage phi29 DNA occurs with translation systems derived from Bacillus subtilis or Escherichia coli. This is in sharp contrast to the strict dependence on ribosome salt wash fract
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8966003d205ac5bc14c878d85a4fb506
https://doi.org/10.1073/pnas.78.8.4912
https://doi.org/10.1073/pnas.78.8.4912
Publikováno v:
Journal of Biological Chemistry. 251:1675-1682
The semisynthetic syntheses and some properties of derivatives of Clostridium acidi-urici ferredoxin that contain amino acid deletions or replacements in the peptide chain are described. All 16 stable derivatives prepared, with the exception of [Trp2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21d007e69843d58f6a4b0f7f70c0a685
https://doi.org/10.1016/s0021-9258(17)33702-x
https://doi.org/10.1016/s0021-9258(17)33702-x
Publikováno v:
Journal of Biological Chemistry. 251:1683-1687
The effects of pH and ionic strength on the midpoint reduction potential (Emp) of Clostridium acidi-urici ferredoxin were determined using hydrogen gas and hydrogenase. The Emp of native ferredoxin at 24-25 degrees in 0.1 M Tris-chloride buffer, pH 7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::211284826f3147d28c48aa78aad1cc84
https://doi.org/10.1016/s0021-9258(17)33703-1
https://doi.org/10.1016/s0021-9258(17)33703-1
Publikováno v:
Journal of Biological Chemistry. 256:11273-11282
A plasmid carrying the Gram-positive Staphylococcus aureus PC1 beta-lactamase gene is active in directing a cell-free transcription and translation system from Bacillus subtilis. The major protein synthesized has been identified as the S. aureus beta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::45d6a1b43c50d871a75425804aa89c2a
https://doi.org/10.1016/s0021-9258(19)68588-1
https://doi.org/10.1016/s0021-9258(19)68588-1
Publikováno v:
Journal of Biological Chemistry. 256:11283-11291
The base sequence of the ribosome binding site region of the Gram-positive Staphylococcus aureus beta-lactamase gene has been determined. The leader peptide sequence of 24 amino acids which precedes the NH2 terminus of extracellular S. aureus beta-la
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5556f6abe56f350820dbb58254af32a4
https://doi.org/10.1016/s0021-9258(19)68589-3
https://doi.org/10.1016/s0021-9258(19)68589-3
Publikováno v:
Journal of Bacteriology. 116:41-47
The NH 2 -terminal amino acid distribution of Streptococcus faecalis R soluble and ribosomal proteins isolated from cells at different stages of growth on either folate-sufficient or folate-deficient medium was determined by the dinitrophenyl method.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::50062a2d0071fb59f9af1e7800a8dec7
https://doi.org/10.1128/jb.116.1.41-47.1973
https://doi.org/10.1128/jb.116.1.41-47.1973
Publikováno v:
Journal of Biological Chemistry. 247:6856-6865
The formation of aminoacyl transfer ribonucleic acid derivatives containing a blocked α-amino group such as the formylmethionyl ester of methionine transfer ribonucleic acid (fMet-tRNAfmet) was studied in Streptococcus faecalis R. This bacterium can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de69c61f17bbe196a3bed1c98df427b3
https://doi.org/10.1016/s0021-9258(19)44664-4
https://doi.org/10.1016/s0021-9258(19)44664-4
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 71(4)
Tyrosyl or other aromatic residues generally occur in two conserved positions in the peptide chain of clostridial-type ferredoxins and have been implicated in the electron transfer function of these iron-sulfur proteins. We have prepared and determin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d406dd16af57e67ad357d361124a0ff
https://pubmed.ncbi.nlm.nih.gov/4364535
https://pubmed.ncbi.nlm.nih.gov/4364535
Publikováno v:
Biochemical and biophysical research communications. 61(1)
Clostridium M-E ferredoxin has been chemically modified by replacing the only aromatic amino acid residue it contains, Tyr2, with leucine. The resulting Clostridium M-E [Leu2]ferredoxin, which is devoid of aromatic amino acid residues, is as active a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e529f73a9d7bf69ec72015381e2b34c1
https://pubmed.ncbi.nlm.nih.gov/4441392
https://pubmed.ncbi.nlm.nih.gov/4441392