Zobrazeno 1 - 10
of 71
pro vyhledávání: '"Barry L. Haymore"'
Publikováno v:
Journal of Chromatography B: Biomedical Sciences and Applications. 584:77-84
Mammalian phosphorylase isozymes from muscle, brain and liver were expressed in Escherichia coli and purified from the crude bacterial cell extracts in one step using a copper-loaded, metal-affinity matrix. Good chromatographic behavior, enzyme activ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd3e6765aa1945bd4c6156a02f8e3e46
https://doi.org/10.1016/0378-4347(92)80011-e
https://doi.org/10.1016/0378-4347(92)80011-e
Autor:
Barry L. Haymore, Richard C. Willson, Ajish Potty, Joseph Y. Fu, Sindhu Balan, George E. Fox, David J. Hill
Publikováno v:
Journal of chromatography. A. 1115(1-2)
Immobilized metal-chelate affinity chromatography has been widely used in the purification of proteins, and we have recently found that it can also be applied to purification of nucleic acids through interactions involving exposed bases, especially p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf81e437a32a3a6d10f2827e57d5ef4d
https://pubmed.ncbi.nlm.nih.gov/16600263
https://pubmed.ncbi.nlm.nih.gov/16600263
Publikováno v:
Biochemistry. 32(8)
The X-ray crystal structure of the copper complex of the rat trypsin mutant Arg96 to His96 (trypsin R96H) has been determined in order to ascertain the nature of the engineered metal-binding site and to understand the structural basis for the metal-i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0e6a24538af6ff9a3ee168e26aef076
https://pubmed.ncbi.nlm.nih.gov/8448149
https://pubmed.ncbi.nlm.nih.gov/8448149
Autor:
Barry L. Haymore, Frances H. Arnold
Publikováno v:
Science (New York, N.Y.). 252(5014)
Proteins can make use of metal ions to bind substrates, to maintain structure, to effect catalysis, and for allosteric control and regulation. In order to hold a particular metal ion with high affinity and specificity, proteins form multidentate bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a45dece3679e6520073a18c493b2d45
https://pubmed.ncbi.nlm.nih.gov/1648261
https://pubmed.ncbi.nlm.nih.gov/1648261
Characterization of His-X3-His sites in alpha-helices of synthetic metal-binding bovine somatotropin
Publikováno v:
Protein engineering. 4(3)
Variants of bovine somatotropin have been engineered to contain synthetic metal-binding sites consisting of two solvent-exposed histidines separated by a single turn of an alpha-helix (His-X3-His variants). The affinities of these proteins for Cu(II)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f4d81a10c9f22820f8dc21498ed3d24c
https://pubmed.ncbi.nlm.nih.gov/1713327
https://pubmed.ncbi.nlm.nih.gov/1713327
Publikováno v:
Proteins. 10(2)
A metal-binding site consisting of two histidines positioned His-X3-His in an alpha-helix has been engineered into the surface of Saccharomyces cerevisiae iso-1-cytochrome c. The synthetic metal-binding cytochrome c retains its biological activity in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::900bae63b563af649b70915595f91ae7
https://pubmed.ncbi.nlm.nih.gov/1654548
https://pubmed.ncbi.nlm.nih.gov/1654548
Publikováno v:
Biochemistry. 29(37)
A recombinant trypsin was designed whose catalytic activity can be regulated by varying the concentration of Cu2+ in solution. Substitution of Arg-96 with a His in rat trypsin (trypsin R96H) places a new imidazole group on the surface of the enzyme n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f5be5081944bdd186b80303ea73643d
https://pubmed.ncbi.nlm.nih.gov/2125468
https://pubmed.ncbi.nlm.nih.gov/2125468
Publikováno v:
J. Chem. Soc., Dalton Trans.. :621-627
Ruthenium and osmium hydridonitrosyl complexes, [MH(NO)(PPh3)3], react with perfluorocarboxylic acids RCO2H (R = CF3 or C2F5) to afford the products [Ru(O2CR)3(NO)(PPh3)2] and [OsH(O2CR)2(NO)(PPh3)2] respectively. The reaction intermediates [RuH(O2CR
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fbf8247ff7379b411a6d343f0e85855
https://doi.org/10.1039/dt9850000621
https://doi.org/10.1039/dt9850000621
Publikováno v:
Journal of the American Chemical Society. 101:2063-2068
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21ba317bc383f4999e92049ac7f5210d
https://doi.org/10.1021/ja00502a021
https://doi.org/10.1021/ja00502a021
Autor:
Barry L. Haymore, James A. Ibers
Publikováno v:
Inorganic Chemistry. 14:2784-2795
Aryldiazo complexes, [M(CO)$sub 2$(NNPh)(PPh$sub 3$)$sub 2$][PF$sub 6$](M = Os, Ru; Ph = C$sub 6$H$sub 5$), were prepared by allowing diazonium salts to react with M(CO)$sub 3$(PPh$sub 3$)$sub 2$. Infrared spectra of the Ru complex suggest the presen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::13699431a670c5940a39d06819804aca
https://doi.org/10.1021/ic50153a038
https://doi.org/10.1021/ic50153a038