Re-evaluation of the role of thiol groups in rabbit muscle aldolase A

1986 ◽  
Vol 874 (3) ◽  
pp. 365-367 ◽  
Author(s):  
Tomasz Heyduk ◽  
Marian Kochman
Keyword(s):  
Rabbit Muscle ◽  
Thiol Groups ◽  
Aldolase A

scholarly journals Mechanism of porphobilinogen synthase. Possible role of essential thiol groups.

1977 ◽  
Vol 252 (24) ◽  
pp. 8965-8974 ◽  
Author(s):  
G.F. Barnard ◽  
R. Itoh ◽  
L.H. Hohberger ◽  
D. Shemin
Keyword(s):  
Thiol Groups ◽  
Porphobilinogen Synthase

On the molecular basis of pyruvate kinase deficiency II. Role of thiol groups in pyruvate kinase from pyruvate kinase-deficient patients

1974 ◽  
Vol 334 (2) ◽  
pp. 361-367 ◽  
Author(s):  
Th.J.C. Van Berkel ◽  
G.E.J. Staal ◽  
J.F. Koster ◽  
J.G. Nyessen ◽  
L. van Milligen-Boersma
Keyword(s):  
Pyruvate Kinase ◽  
Molecular Basis ◽  
Thiol Groups ◽  
Pyruvate Kinase Deficiency

scholarly journals A combination of MEF3 and NFI proteins activates transcription in a subset of fast-twitch muscles.

1997 ◽  
Vol 17 (2) ◽  
pp. 656-666 ◽  
Author(s):  
F Spitz ◽  
M Salminen ◽  
J Demignon ◽  
A Kahn ◽  
D Daegelen ◽  
...  
Keyword(s):  
Regulatory Elements ◽  
Specific Expression ◽  
Transgenic Lines ◽  
Slow Twitch ◽  
Myogenic Factors ◽  
Fast Twitch ◽  
Restricted Pattern ◽  
Aldolase A ◽  
Drive Reporter Gene Expression

The human aldolase A pM promoter is active in fast-twitch muscles. To understand the role of the different transcription factors which bind to this promoter and determine which ones are responsible for its restricted pattern of expression, we analyzed several transgenic lines harboring different combinations of pM regulatory elements. We show that muscle-specific expression can be achieved without any binding sites for the myogenic factors MyoD and MEF2 and that a 64-bp fragment comprising a MEF3 motif and an NFI binding site is sufficient to drive reporter gene expression in some but, interestingly, not all fast-twitch muscles. A result related to this pattern of expression is that some isoforms of NFI proteins accumulate differentially in fast- and slow-twitch muscles and in distinct fast-twitch muscles. We propose that these isoforms of NFI proteins might provide a molecular basis for skeletal muscle diversity.

scholarly journals Oxidation of human haemoglobin by copper. Mechanism and suggested role of the thiol group of residue β-93

1977 ◽  
Vol 165 (1) ◽  
pp. 141-148 ◽  
Author(s):  
C C Winterbourn ◽  
R W Carrell
Keyword(s):  
Electron Transfer ◽  
Binding Sites ◽  
Equilibrium Dialysis ◽  
Thiol Group ◽  
Thiol Groups ◽  
Human Haemoglobin ◽  
High Affinity ◽  
Rate Determining Step ◽  
Haemoglobin Molecule

Addition of Cu(II) ions to human oxyhaemoglobin caused the rapid oxidation of the haem groups of the beta-chain. Oxidation required binding of Cu(II) to sites involving the thiol group of beta-93 residues and was prevented when these groups were blocked with iodoacetamide or N-ethylmaleimide. Equilibrium-dialysis studies showed three pairs of binding sites, two pairs with high affinity for Cu(II) and one pair with lower affinity. It was the second pair of high-affinity sites that were blocked with iodoacetamide and were involved in haem oxidation. Cu(II) oxidized deoxyhaemoglobin at least ten times as fast as oxyhaemoglobin, and analysis of rates suggested that binding rather than electron transfer was the rate-determining step. No thiol-group oxidation to disulphides occurred during the period of haem oxidation, although it did occur subsequently in the presence of oxygen, or when Cu(II) was added to methaemoglobin. It is proposed that thiol oxidation did not occur because there exists a pathway of electron transfer between the haem group and copper bound to the beta-93 thiol groups. The route for this electron transfer is discussed, as well as the implications as to the function of the beta-93 cysteine in the haemoglobin molecule.

scholarly journals The Role of Xanthine Oxidase in Hemodialysis-Induced Oxidative Injury: Relationship with Nutritional Status

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Dijana Miric ◽  
Bojana Kisic ◽  
Radojica Stolic ◽  
Bratislav Miric ◽  
Radoslav Mitic ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Risk Index ◽  
Oxidative Injury ◽  
Chronic Hemodialysis ◽  
Nutritional Risk ◽  
Lipid Hydroperoxides ◽  
Thiol Groups ◽  
Nutritional Risk Index ◽  
Baseline Values

The role of xanthine oxidase (XOD) in patients undergoing chronic hemodialysis treatment (HD) is poorly understood. Geriatric nutritional risk index (GNRI) ≤ 90 could be linked with malnutrition-inflammation complex syndrome. This study measured XOD, myeloperoxidase (MPO), superoxide dismutase (SOD), lipid hydroperoxides, total free thiol groups, and advanced oxidation protein products (AOPP) in 50 HD patients before commencing (pre-HD) and immediately after completion of HD session (post-HD) and in 22 healthy controls. Pre-HD serum hydroperoxides, AOPP, XOD, and SOD were higher and total thiol groups were lower in patients than in controls (P<0.05, resp.). Compared to baseline values, serum MPO activity was increased irrespective of GNRI status. Serum XOD activity was increasing during HD treatment in the group with GNRI ≤ 90 (P=0.030) whilst decreasing in the group with GNRI > 90 (P=0.002). In a multiple regression analysis, post-HD serum XOD activity was independently associated with GNRI ≤ 90 (β  ± SE: 0.398 ± 0.151;P=0.012) and HD vintage (β  ± SE: −0.349 ± 0.139;P=0.016). These results indicate that an upregulated XOD may be implicated in HD-induced oxidative injury contributing to accelerated protein damage in patients with GNRI ≤ 90.

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