Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Judith Rittenhouse"'
Autor:
Richard A. Pittner, Kevin Beaumont, Candace X. Moore, Keith Albrandt, Judith Rittenhouse, Joy E. Koda, Laurie S. L. Gaeta, Timothy J. Rink
Publikováno v:
Journal of Cellular Biochemistry. 55:19-28
Amylin is a 37-amino acid peptide first isolated, purified, and characterized from the amyloid deposits in the pancreases of type 2 diabetics. It is synthesized and secreted primarily from pancreatic beta cells along with insulin. The ability of amyl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0cb875f0166b9e8fbeadc159b8b06ff9
https://doi.org/10.1002/jcb.240550004
https://doi.org/10.1002/jcb.240550004
Publikováno v:
Journal of Biological Chemistry. 266:19217-19220
We report the first direct observation of the subunit self-association behavior of highly purified recombinant human immunodeficiency virus type-2 (HIV-2) proteinase. Multiple samples of enzyme were subjected to sedimentation equilibrium analytical u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9d111ca77e89594ad2094c791a93d906
https://doi.org/10.1016/s0021-9258(18)54985-1
https://doi.org/10.1016/s0021-9258(18)54985-1
Autor:
Kathryn S. Albrecht, Robert L. Simmer, William E. Kohlbrenner, Mary C. Turon, John W. Erickson, Debra Weigl, Federico Mordini, Judith Rittenhouse, Rosalind Helfrich
Publikováno v:
Biochemical and Biophysical Research Communications. 171:60-66
A procedure is described which employs pepstatin-agarose for the affinity purification of either HIV-1 or HIV-2 protease from two similar recombinant E. coli constructs that were developed for the expression of these enzymes. HIV-2 protease was routi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c2c1f8ac2c75c5070a7b9f37a5959b1
https://doi.org/10.1016/0006-291x(90)91356-w
https://doi.org/10.1016/0006-291x(90)91356-w
Publikováno v:
Journal of Biological Chemistry. 262:10114-10119
In vivo labeled fructose-1,6-bisphosphatase was immunopurified from yeast (Saccharomyces cerevisiae) cells that had been incubated in the presence of [32P] orthophosphate. Tryptic peptides from labeled enzyme were mapped by high performance liquid ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e628d01e3e8f6135f599f6ba957d537
https://doi.org/10.1016/s0021-9258(18)61085-3
https://doi.org/10.1016/s0021-9258(18)61085-3
Publikováno v:
Journal of Biological Chemistry. 258:7648-7652
Studies of in vitro phosphorylation of four different gluconeogenic fructose-1,6-bisphosphatases by the catalytic subunit of cyclic AMP-dependent protein kinase have shown that only rat liver fructose-1,6-bisphosphatase is a substrate of the protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d4349898ccf7064aad84e4b974a8aa34
https://doi.org/10.1016/s0021-9258(18)32228-2
https://doi.org/10.1016/s0021-9258(18)32228-2
Publikováno v:
Proceedings of the National Academy of Sciences. 77:6086-6090
Total RNA, prepared from immature or mature mouse testes or from spermatogenic cells separated on the basis of sedimentation velocity, was translated in vitro. Mouse protamine-like histone could be identified as an in vitro translational product when
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c003c2d9ff5cff18076c736625ab996f
https://doi.org/10.1073/pnas.77.10.6086
https://doi.org/10.1073/pnas.77.10.6086
Publikováno v:
Journal of Biological Chemistry. 263:6058-6062
The properties of dephospho- and phosphofructose-1,6-bisphosphatase from the yeast Saccharomyces cerevisiae and of two mutant enzymes in which the phosphorylatable Ser11 had been changed by site-directed mutagenesis (Ser—-Ala and Ser—-Asp) were s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b15ef9ef9b4a89d11dc5b0f522f4145d
https://doi.org/10.1016/s0021-9258(18)68748-4
https://doi.org/10.1016/s0021-9258(18)68748-4
Publikováno v:
Journal of Biological Chemistry. 261:3939-3943
Fructose-1,6-bisphosphatase from the yeast Saccharomyces cerevisiae has properties similar to other gluconeogenic fructose-1,6-bisphosphatases, but an unusual characteristic of the yeast enzyme is that it can be phosphorylated in vitro by cAMP-depend
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::785fe40fe2ffd86ca09a9e43af8ab68d
https://doi.org/10.1016/s0021-9258(17)35605-3
https://doi.org/10.1016/s0021-9258(17)35605-3
Publikováno v:
Biochemical and Biophysical Research Communications. 119:1103-1108
Fructose 2,6-bisphosphate, a potent inhibitor of fructose-1,6-bisphosphatases, was found to be an inhibitor of the Escherichia coli enzyme. The substrate saturation curves in the presence of inhibitor were sigmoidal and the inhibition was much strong
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41bdb46874875bcafddf61c41736ba28
https://doi.org/10.1016/0006-291x(84)90888-x
https://doi.org/10.1016/0006-291x(84)90888-x
Publikováno v:
Journal of Biological Chemistry. 259:3831-3833
Rat liver fructose 1,6-bisphosphatase appears to be unique in that it extends 24-26 residues beyond the COOH-terminal amino acid of other mammalian fructose 1,6-bisphosphatases and this extension contains phosphorylation sites. Using as a frame of re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eb50c60cb87edd1616bd54deda266e0a
https://doi.org/10.1016/s0021-9258(17)43171-1
https://doi.org/10.1016/s0021-9258(17)43171-1