Location of the reactive sulphydryl group in human globin

1973 ◽  
Vol 38 (2) ◽  
pp. 465-467
Author(s):  
J. Sojka ◽  
Z. Hrkal ◽  
Z. Vodrážka
Keyword(s):  
Sulphydryl Group

Covalent binding of catechols to proteins through the sulphydryl group

1988 ◽  
Vol 37 (9) ◽  
pp. 1707-1710 ◽  
Author(s):  
Shosuke Ito ◽  
Toshiaki Kato ◽  
Keisuke Fujita
Keyword(s):  
Covalent Binding ◽  
Sulphydryl Group

A Study of the "Lipoxidase" in the Flesh of British Columbia Herring

1952 ◽  
Vol 9 (8) ◽  
pp. 393-416 ◽  
Author(s):  
M. M. R. Khan
Keyword(s):  
British Columbia ◽  
Unsaturated Fatty Acids ◽  
Dark Muscle ◽  
Active Centre ◽  
Nitrogenous Compounds ◽  
Sulphydryl Group ◽  
Optimal Activity ◽  
Highly Active ◽  
Enzyme Substrate ◽  
Kinetics Of

From the dark muscle of British Columbia herring a highly active enzyme capable of peroxidizing non-conjugated unsaturated fatty acids was isolated. This "lipoxidase", which was shown to be a nitrogenous complex possessing no heavy metals or sulphydryl group as the active centre, is heat-labile and can act only in presence of activators such as certain iron-containing organic nitrogenous compounds. Two such compounds, namely haemoglobin and cytochrome "c" were isolated. The enzyme exhibits optimal activity at 15 °C. and pH 6.9. There is also an optimal concentration of enzyme, substrate, and of the activators for maximal enzyme activity. The presence of the activators appears to change the kinetics, of the reactions. The inhibition of the enzymic reaction brought about by cyanide and azide is possibly due to the inactivation of the iron-containing activators rather than of the enzyme itself.

Reduction of Selenites and Tellurites by the Sulphydryl Group

1934 ◽  
Vol 31 (9) ◽  
pp. 1092-1094 ◽  
Author(s):  
V. E. Levine ◽  
B. M. Rosenthal
Keyword(s):  
Sulphydryl Group

IV. Cysteine proteinases

1970 ◽  
Vol 257 (813) ◽  
pp. 231-236 ◽  
Keyword(s):  
Oxidation State ◽  
Proteolytic Enzyme ◽  
Enzyme Preparation ◽  
Chemical Nature ◽  
Enzymic Activity ◽  
Active Enzyme ◽  
Tropical Tree ◽  
Cysteine Proteinases ◽  
Sulphydryl Group ◽  
Sh Group

Papain (EC 3.4.4.10) is a proteolytic enzyme which is isolated from the Papaya, a common tropical tree. It is a sulphydryl enzyme and its SH group is required for enzymic activity. Papain as usually prepared (Kimmel & Smith 1954) contains only a small portion of active molecules. The majority of the molecules are inactive because their sulphydryl group is blocked. Part of the blocking is caused by disulphide formation with cysteine (Sluyterman 1967). This disulphide can be reduced by an excess of cysteine resulting in an active enzyme preparation. The free SH content never reaches 100% and is often not more than about 50% , so that we must distinguish between papain molecules with a reversibly and an irreversibly blocked SH group. The chemical nature of the irreversible blocking is not yet known. It might well be due to a higher oxidation state of the sulphur which cannot be reduced by an excess of cysteine (Glazer & Smith 1965).

scholarly journals Concentration and reactivity of the sulphydryl group population on the membrane of intact erythrocytes in patients with rheumatoid arthritis.

1990 ◽  
Vol 49 (9) ◽  
pp. 668-671 ◽  
Author(s):  
C Chilles ◽  
M Mulheron ◽  
F M McCrae ◽  
J Reglinksi ◽  
W E Smith ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Sulphydryl Group ◽  
Group Population
Sign in / Sign up

Export Citation Format

Share Document