نتایج جستجو برای: homotropic effect

تعداد نتایج: 1641742  

Ashraf Shabani Marzieh Dehghan Shasaltaneh Masoumeh Tayari, Mostafa Rezaei-Tavirani S. Zahra Moosavi-Nejad

Haptoglobin (Hp) is a mammalian serum glycoprotein showing a genetic polymorphism with three types, 1-1, 2-2 and 1-2. Hp appears to conserve the recycling of heme-iron by forming an essentially irreversible but non-covalent complex with hemoglobin which is released into the plasma by erythrocyte lysis. As an important consequence, Haptoglobin-Hemoglobin complex (Hp-Hb) shows considerable antiox...

Journal: :iranian journal of pharmaceutical research 0
masoumeh tayari department of biology, faculty of basic sciences, alzahra university, 1993891176, tehran, iran. s. zahra moosavi-nejad department of biology, faculty of basic sciences, alzahra university, 1993891176, tehran, iran. ashraf shabani department of biology, faculty of basic sciences, alzahra university, 1993891176, tehran, iran mostafa rezaei-tavirani proteomics research center, faculty of paramedical sciences, shahid beheshti university of medical sciences, tehran, iran. asre novin institute of research and industrial services, tehran, iran. marzieh dehghan shasaltaneh department of biology, faculty of basic sciences, alzahra university, 1993891176, tehran, iran

haptoglobin (hp) is a mammalian serum glycoprotein showing a genetic polymorphism with three types, 1-1, 2-2 and 1-2. hp appears to conserve the recycling of heme-iron by forming an essentially irreversible but non-covalent complex with hemoglobin which is released into the plasma by erythrocyte lysis. as an important consequence, haptoglobin-hemoglobin complex (hp-hb) shows considerable antiox...

Journal: :The Journal of biological chemistry 1970
J H Wang J I Tu

The kinetic properties of a glutaraldehyde-modified phosphorylase b have been examined to understand further the mechanism of allosteric transition of this enzyme. The sigmoidal response to AMP, which is observed with native glycogen phosphorylase b, cannot be demonstrated with the modified enzyme. This enzyme derivative also exhibits no homotropic cooperativity of glucose 1 -phosphate under co...

Journal: :The Journal of biological chemistry 1977
E R Kantrowitz W N Lipscomb

The reaction of phenylglyoxal with aspartate transcarbamylase and its isolated catalytic subunit results in complete loss of enzymatic activity (Kantrowitz, E. R., and Lipscomb, W. N. (1976) J. Biol. Chem. 251, 2688-2695). If N-(phosphonacetyl)-L-aspartate is used to protect the active site, we find that phenylglyoxal causes destruction of the enzyme's susceptibility to activation by ATP and in...

Journal: :The Journal of biological chemistry 1989
T S Corder J R Wild

The substitution of alanine for lysine at position 56 of the regulatory polypeptide of aspartate transcarbamoylase affected both homotropic and heterotropic characteristics. In the absence of effectors, the ALAr56-substituted holoenzyme lost the homotropic cooperativity observed for aspartate in the wild-type holoenzyme. Under conditions of allosteric inhibition in the presence of 2mM CTP, the ...

2003
T. G. LESSIE

Two major species of glucose-6-phosphate dehydrogenase (EC 1.1.1.49) differing in size, pyridine nucleotide specificity, and susceptibility to inhibition by adenosine 5'-triphosphate (ATP) were detected in extracts of Pseudomonas multivorans (which has recently been shown to be synonymous with the species Pseudomonas cepacia) ATCC 17616. The large species (molecular weight ca. 230,000) was acti...

Journal: :Archives of Biochemistry and Biophysics 2012

2011
Masoumeh Tayari Zahra Moosavi-Nejad Fatemeh Moosavi Nejad Mostafa Rezaei-Tavirani Marzieh Dehghan Shasaltaneh

Haptoglobin (Hp) is a mammalian serum glycoprotein showing a genetic polymorphism with three types, 1-1, 2-2 and 1-2. Hp appears to conserve the recycling of heme-iron by forming an essentially irreversible but non-covalent complex with hemoglobin which is released into the plasma by erythrocyte lysis. As an important consequence, Haptoglobin-Hemoglobin complex (Hp-Hb) shows considerable antiox...

Journal: :The Journal of biological chemistry 2002
Takashi Yonetani Sung-Ick Park Antonio Tsuneshige Kiyohiro Imai Kenji Kanaori

The O(2) equilibria of human adult hemoglobin have been measured in a wide range of solution conditions in the presence and absence of various allosteric effectors in order to determine how far hemoglobin can modulate its O(2) affinity. The O(2) affinity, cooperative behavior, and the Bohr effect of hemoglobin are modulated principally by tertiary structural changes, which are induced by its in...

Journal: :Bioscience, biotechnology, and biochemistry 2005
Qing-Shan Li Jun Ogawa Rolf D Schmid Sakayu Shimizu

Cytochrome P450 BM-3 from Bacillus megaterium catalyzed NADPH-supported indole hydroxylation under alkaline conditions with homotropic cooperativity toward indole. The activity was also found with the support of H2O2, tert-butyl hydroperoxide (tBuOOH), or cumene hydroperoxide (CuOOH). Enhanced activity and heterotropic cooperativity were observed in CuOOH-supported hydroxylation, and both the H...

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