Effect of Oxidation and Serum Dialyzate on the-SH Groups of Lens Protein Fractions and Serum Albumin1

2015 ◽  
pp. 450-453
Author(s):  
C. Fiore ◽  
N. Bocci ◽  
M. Testa
Keyword(s):  
Protein Fractions ◽  
Lens Protein ◽  
Sh Groups

Cataract Induction by 1,2-Naphthoquinone II. Mechanism of Hydrogenperoxide Formation and Inhibition by Iodide

1991 ◽  
Vol 46 (3-4) ◽  
pp. 285-290
Author(s):  
R. Kroner ◽  
E. Kleber ◽  
E. F. Elstner
Keyword(s):  
Oxygen Uptake ◽  
Protein Modification ◽  
Oxygen Activation ◽  
Redox Cycling ◽  
Lens Protein ◽  
Dependent Manner ◽  
Yield Losses ◽  
Concentration Dependent Manner ◽  
Glutathione Conjugation ◽  
Sh Groups

Naphthalene cataract is probably due to peroxide production through naphthoquinone (NQ) redox cycling and/or glutathione conjugation. Both mechanisms yield losses of essential SH-groups in cristallins and are thus probably involved in protein modification finally visible as lens opacity. 1,2-N aphthoquinone produces H2O2 in the presence of either ascorbate, glutathione, NADH or - to a lesser extend - by homogenates of lens protein preparations. In the presence of 1,2-naphthoquinone and the above reductive additions, both, oxygen uptake and H2O2 formation can be observed. Reductive oxygen activation in these systems are diminuated by iodide in a concentration-dependent manner. Since maleimide-treated proteins are less capable to activate oxygen by 1,2-naphthoquinone, a direct oxygen activation by the interactions of 1,2-naphthoquinone with protein-SH is indicated. Catalysis of “diaphorase”-type (dia) enzymes via NADH - dia - 1,2-NQ - O2 seems not to operate in hydrogenperoxide production during 1,2-naphthoquinone lens toxicity.

scholarly journals SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS

1936 ◽  
Vol 19 (3) ◽  
pp. 439-450 ◽  
Author(s):  
A. E. Mirsky ◽  
M. L. Anson
Keyword(s):  
Crystalline Lens ◽  
Iron Porphyrin ◽  
Lens Protein ◽  
Native State ◽  
Lens Proteins ◽  
Sh Groups ◽  
Ph Range

Hemoglobin and the proteins of the crystalline lens contain active SH groups while in the native state, the number of active groups increasing as the pH rises. All the SH groups of denatured globin and of the denatured lens proteins are active at a pH so low that practically none of the SH groups of native hemoglobin and of native lens protein are active. The effect of denaturation on the SH groups of a protein is to extend towards the acid side the pH range of their activity. It is possible to oxidize the iron-porphyrin and the SH groups of hemoglobin independently of each other.

scholarly journals The effect of prednisolone on the course of myocardial infarction

1981 ◽  
Vol 62 (5) ◽  
pp. 14-18
Author(s):  
Z. S. Khasanov
Keyword(s):  
Myocardial Infarction ◽  
Beneficial Effect ◽  
Serum Enzymes ◽  
Protein Fractions ◽  
Complex Treatment ◽  
Sh Groups ◽  
Daily Urine ◽  
Natriuretic Effect

85 patients with large-focal myocardial infarction aged from 38 to 72 years were examined. All patients received complex treatment, and 42 of them received additional prednisolone at a dose of 20-25 mg per day by mouth in the first 6-8 days from the onset of the disease. Studies have shown that the inclusion of prednisolone in the treatment complex has a beneficial effect on the course of myocardial infarction: it accelerates the normalization of protein SH-groups, protein fractions, serum enzymes, electrolytes in the blood and catecholamines in daily urine, gives a diuretic and natriuretic effect without causing an increase in caliuresis.

scholarly journals SULFHYDRYL AND DISULFIDE GROUPS OF PROTEINS

1936 ◽  
Vol 19 (4) ◽  
pp. 559-570 ◽  
Author(s):  
A. E. Mirsky
Keyword(s):  
Skeletal Muscle ◽  
Crystalline Lens ◽  
Protein Fractions ◽  
Sh Groups ◽  
Denatured Protein ◽  
Native Proteins ◽  
Denatured Proteins ◽  
Single Exception ◽  
Minced Muscle

1. In the denatured proteins of skeletal muscle, the ratio of SH to S-S groups is higher than in the mixed denatured proteins of other tissues, with a single exception—the proteins of the crystalline lens. 2. The number of active SH groups in the proteins of minced muscle or in any of the protein fractions of muscle is only a fraction of the number found after the proteins have been treated with a denaturing agent. 3. The SH groups of the native proteins of muscle are activated by a rise in pH. 4. The relation between pH and number of active SH groups in the proteins of minced muscle and in the various protein fractions of muscle shows that little, if any, denatured protein is present in minced muscle.

Antigenic protein fractions reacting with sera of sparganosis patients

1988 ◽  
Vol 26 (3) ◽  
pp. 163 ◽  
Author(s):  
Sung Ho Choi ◽  
Shin Yong Kang ◽  
Yoon Kong ◽  
Seung Yull Cho
Keyword(s):  
Protein Fractions ◽  
Antigenic Protein

Isolation of casein protein fractions

2017 ◽  
Vol 1 (1) ◽  
Author(s):  
Zeynep Atamer ◽  
Katharina Thienel ◽  
Aline Holder ◽  
Thomas Schubert ◽  
Remko Boom ◽  
...  
Keyword(s):  
Protein Fractions ◽  
Casein Protein
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