Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Mirna, Flogel"'
Publikováno v:
Acta pharmaceutica (Zagreb, Croatia). 56(1)
Glycans are the most abundant and most diverse biopolymers in nature. Because of their highly specific interactions with physiological receptors, they participate in many crucial biological processes. All these processes are potential targets for the
The steady-state kinetics of alkaline phosphatase from E. coli performed with pNPP as a substrate have been investigated. The enzyme shows deviation from Michaelis-Menten kinetics giving concave down Hanes plots. In the presence of a competitive subs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=57a035e5b1ae::192967eb7e5b479cb7b1a3a7937b0600
https://www.bib.irb.hr/982107
https://www.bib.irb.hr/982107
Autor:
John F. Halsey, Barbara E. C. Banks, John Walker, Paolo Fasella, Patricia B. Porter, Emilia Chiancone, Shawn Doonan, Thomas H. Crouch, Charles A. Vernon, Mirna Flogel
Publikováno v:
European Journal of Biochemistry. 71:469-473
The isopotential specific volume of cytoplasmic aspartate aminotransferase from pig heart was found to be 0.763 ml g-1 whereas the value of the apparent specific volume obtained by summation of contributions from each type of amino acid in the protei
Autor:
Rodney L. Biltonen, Mirna Flogel
Publikováno v:
Biochemistry. 14:2603-2609
The proton association behavior of ribonuclease A and its complex with 3'-cytosine monophosphate has been thermodynamically characterized in the pH range 4--8 at 25 degrees, mu = 0.05. Calorimetric and potentiometric titration data have been used to
Autor:
Mirna Flogel, Rodney L. Biltonen
Publikováno v:
Biochemistry. 14(12)
The apparent free energy (deltaGapp) and enthalpy changes (deltaHB) associated with the interaction of 3'-cytosine monophosphate (3'-CMP) and ribonuclease A (RNase) are reported for the pH range 4--9, T = 25 degrees, mu = 0.05. The pH dependence of d
Autor:
Mirna Flogel, Tihana Žanić
Publikováno v:
Croatica Chemica Acta
Volume 58
Issue 1
Volume 58
Issue 1
The equilibrium system ribonuclease A-cytidine 3'-monophosphate at pH 5.5, was submitted to thermal perturbation. A derivative fractional degree of saturation with respect to a temperature raise of twenty degrees was recorded as a function of free li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::3120c8050967c09653897b44fdfc4c1a
https://repozitorij.pharma.unizg.hr/islandora/object/pharma:1480/datastream/FILE0
https://repozitorij.pharma.unizg.hr/islandora/object/pharma:1480/datastream/FILE0
Publikováno v:
Biochemistry. 14(12)
It is demonstrated that a model of nucleotide binding to ribonuclease A similar to that proposed by Hammes and coworkers (G. G. Hammes (1968), Adv. Protein Chem. 23, 1) is at least, approximately applicable for both cyclic nucleotide substrates and m
Autor:
Balen, Biljana, Krsnik-Rasol, Marijana, Milošević, Jadranka, Vakhrushev, Sergey, Peter-Katalinić, Jasna
N-glycosylation of proteins has been intensively investigated during past decades in context of its influence to correct folding, biological activity and stability of proteins. Little information, however, is available about the N-glycoprotein patter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=57a035e5b1ae::63420e75150cbcc8f16d369ce5778861
https://www.bib.irb.hr/198492
https://www.bib.irb.hr/198492
• determination of the most frequent TPMT allelic polymorphism • estimation of the concordance rate between red blood cell (RBC) thiopurime S- methyltransferase (TPMT ; EC 2.1.1.67) activity and genotype in TPMT locus (mutations and/or polymorphi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=57a035e5b1ae::884222c4972d85406b69ce759aafe8f6
https://www.bib.irb.hr/500720
https://www.bib.irb.hr/500720
The aminoacyl-tRNA synthetases play a crucial role in protein biosynthesis by specifically charging tRNAs with their cognate amino acids.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=57a035e5b1ae::9cd132764eb660b9c6c98da5ae2740ce
https://www.bib.irb.hr/803172
https://www.bib.irb.hr/803172