Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Elizabeth, Hubert"'
Autor:
Elizabeth, Hubert, Joyce E, Dains
Publikováno v:
Journal of the Advanced Practitioner in Oncology. 13:695-704
Purpose: The purpose of this integrative review was to establish the role of cardiac rhythm analysis (electrocardiogram; EKG) and echocardiogram in increasing clinical suspicion for and earlier diagnosis of cardiac amyloidosis. Methods: A literature
Autor:
Elizabeth, Hubert
Publikováno v:
Revue de l'infirmiere. (140)
Publikováno v:
Revista latinoamericana de microbiologia. 44(1)
The bacteriocin PsVP-10 is a 2.6 Kda peptide which was isolated and purified from Pseudomonas sp. This bacteriocin possesses lethal activity over Enterococcus faecalis, Salmonella typhimurium and Shigella flexneri. The experimental assays showed that
Publikováno v:
Revista latinoamericana de microbiologia. 46(3-4)
The principal aim of this work was to detect the bacteriocinogenic capacity of S. flexneri strains on members of the human intestinal flora. A total of 49 bacteriocinogenic S. flexneri strains were isolated from individuals of both sexes and differen
Publikováno v:
Journal of protein chemistry. 18(5)
Selective treatment of pig kidney fructose 1,6-bisphosphatase with cyanate leads to the formation of an active carbamoylated derivative that shows no cooperative interaction between the AMP-binding sites, but completely retains the sensitivity to the
Autor:
Elizabeth Hubert, Larry Kahn
Publikováno v:
Regional Anesthesia and Pain Medicine. 23:111-112
Publikováno v:
FEBS Letters. 102:29-32
The gluconeogenetic enzyme, fructose 1 ,&bisphosphatase (FDPase) is composed of 4 subunits ]I]. Each subunit has an allosteric site for AMP at neutral pH [2]. The enzyme is also activated by monovalent cations such as K’ and NH: [3]. The specific i
Publikováno v:
Journal of Protein Chemistry. 2:437-443
Selective treatment of pig kidney fructose 1,6-bisphosphatase with potassium cyanate leads to the formation of an active carbamylated enzyme that has lost the cooperative interactions among AMP sites, but retains sensitivity to inhibition of catalyti
Publikováno v:
Journal of Biological Chemistry. 259:723-728
The cytoplasmic isozyme of aspartate transaminase is inactivated by trypsin due to loss of a 19-residue peptide from the NH2-terminal region. A second peptide bond at Arg-25 is then cleaved by trypsin leaving a residual core protein, transaminase 26-
Publikováno v:
Journal of Biological Chemistry. 262:8451-8454
Limited treatment of native pig kidney fructose-1,6-bisphosphatase (50 microM enzyme subunit) with [14C]N-ethylmaleimide (100 microM) at 30 degrees C, pH 7.5, in the presence of AMP (200 microM) results in the modification of 1 reactive cysteine resi