scholarly journals The disulphide bonds of human and rabbit γ-globulins

1965 ◽  
Vol 97 (2) ◽  
pp. 569-572 ◽  
Author(s):  
R Cecil ◽  
GT Stevenson
Keyword(s):  
Heavy Metal ◽  
Gamma Globulin ◽  
Sh Groups ◽  
Predominant Species ◽  
Disulphide Bonds ◽  
Γ Globulins ◽  
Presence And Absence ◽  
Metal Reagents

1. The reaction of the disulphide bonds of the predominant species of human and rabbit gamma-globulins (the 7s gamma-globulins) with sulphite was studied in the presence and absence of denaturing agents and heavy-metal reagents. 2. The total number of bonds reacting/mol. of mol.wt. 160000 was approx. 18 for human and 20 for rabbit gamma-globulin. 3. Six S.S bonds/mol. of human and 6.5 S.S bonds/mol. of rabbit gamma-globulin reacted with sulphite alone at pH6. These appeared to include all the interchain S.S bonds. 4. The number of free SH groups was less than 0.2/mol. of human and less than 0.3/mol. of rabbit gamma-globulin.

scholarly journals Effects of heavy metal on rat liver microsomal Ca2(+)-ATPase and Ca2+ sequestering. Relation to SH groups.

1990 ◽  
Vol 265 (4) ◽  
pp. 2184-2189
Author(s):  
G H Zhang ◽  
M Yamaguchi ◽  
S Kimura ◽  
S Higham ◽  
N Kraus-Friedmann
Keyword(s):  
Heavy Metal ◽  
Rat Liver ◽  
Sh Groups

scholarly journals ENZYMATICALLY PRODUCED SUBUNITS OF PROTEINS FORMED BY PLASMA CELLS IN MICE

1962 ◽  
Vol 115 (3) ◽  
pp. 623-639 ◽  
Author(s):  
J. L. Fahey ◽  
Brigitte A. Askonas
Keyword(s):  
Electrophoretic Mobility ◽  
Gel Electrophoresis ◽  
Gamma Globulin ◽  
Immunological Methods ◽  
Antigenic Determinants ◽  
Antibody Activity ◽  
Starch Gel Electrophoresis ◽  
Myeloma Protein ◽  
Γ Globulins ◽  
Starch Gel

Gamma globulin and antibody obtained from inbred C3H mice are split by papain and cysteine into fragments roughly one-third the size of the original Molecule (S20,w = 3.5S). The papain digests were characterized by starch gel electrophoresis and immunological methods. The highly heterogeneous fragments could be divided into two groups with distinct antigenic determinants (S and F), which were separated by DEAE ion-exchange cellulose chromatography. Approximately two-thirds of the fragments had S antigenic groupings and one-third had F antigenic groupings. These data are consistent with the view that mouse gamma globulin is split by papain and cysteine into three major fragments, two of which are of the S type and one of the F type. Antibody activity of the original molecule was present in the S fragments. Although the S fragments did not precipitate the antigen (hemocyanin) they were shown to bind antigen specifically in the manner of univalent antibodies. The S fragments of normal γ-globulin were very heterogeneous with a broad spectrum of electrophoretic mobilities. Comparison of S fragments from slow and fast migrating globulins showed that the mobilities of the original γ-globulin samples were largely reflected in the mobilities of their S fragments. Additional observations indicated that the F fragments also may help to determine the electrophoretic mobility of intact γ-globulin molecules. S fragments of differing electrophoretic mobility were shown to have the same antigenic determinants, indicating that the structural differences responsible for the electrophoretic mobility differences were not involved in the antigenic groupings identified with rabbit antisera. The F fragments of normal γ-globulin migrated more rapidly than the S fragments, were less heterogeneous, and showed several bands on starch gel electrophoresis. The F fragments differed antigenically from the S fragments, and had no antibody activity. Two groups of F fragments (F and F') were detected with some antisera. The γ-myeloma protein (5563) formed in a C3H plasma cell tumor and similarly fragmented by treatment with papain and cysteine, produced much more discrete S and F components than were found in the normal γ-globulin digest. The electrophoretic properties of the myeloma protein fragments were within the range observed for normal γ-globulin fragments. Although the γ-myeloma protein shares antigenic determinants with normal γ-globulins it lacks some of the antigenic groupings present in the γ-globulin preparation. Both S and F fragments from the myeloma protein share antigenic determinants with the corresponding fragments from normal γ-globulin. In addition, both S and F fragments of normal γ-globulin possess antigenic groupings not present in fragments of the γ-myeloma protein, accounting for the antigenic deficiency observed on comparison of the γ-myeloma protein with normal γ-globulins.

scholarly journals Protein thiolation and reversible protein-protein conjugation. N-Succinimidyl 3-(2-pyridyldithio)propionate, a new heterobifunctional reagent

1978 ◽  
Vol 173 (3) ◽  
pp. 723-737 ◽  
Author(s):  
J Carlsson ◽  
H Drevin ◽  
R Axén
Keyword(s):  
Gamma Globulin ◽  
De Novo ◽  
Ester Group ◽  
Alpha Amylase ◽  
Amino Groups ◽  
Protein Conjugates ◽  
Disulphide Bonds ◽  
Concomitant Reduction ◽  
Antibody Conjugate ◽  
Aliphatic Thiols

A heterobifunctional reagent, N-succinimidyl 3-(2-pyridyldithio)propionate, was synthesized. Its N-hydroxysuccinimide ester group reacts with amino groups and the 2-pyridyl disulphide structure reacts with aliphatic thiols. A new thiolation procedure for proteins is based on this reagent. The procedure involves two steps. First, 2-pyridyl disulphide structures are introduced into the protein by the reaction of some of its amino groups with the N-hydroxysuccinimide ester sie of the reagent. The protein-bound 2-pyridyl disulphide structures are then reduced with dithiothreitol. This reaction can be carried out without concomitant reduction of native disulphide bonds. The technique has been used for the introduction of thiol groups de novo into ribonuclease, gamma-globulin, alpha-amylase and horseradish peroxidase. N-Succinimidyl 3-(2-pyridyldithio)propionate can also be used for the preparation of protein-protein conjugates. This application is based on the fact that protein-2-pyridyl disulphide derivatives (formed from the reaction of non-thiol proteins with the reagent) react with thiol-containing proteins (with native thiols or thiolated by, for example, the method described above) via thiol-disulphide exchange to form disulphide-linked protein-protein conjugates. This conjugation technique has been used for the preparation of an alpha-amylase-urease, a ribonuclease-albumin and a peroxidase-rabbit anti-(human transferrin) antibody conjugate. The disulphide bridges between the protein molecules can easily be split by reduction or by thiol-disulphide exchange. Thus conjugation is reversible. This has been demonstrated by scission of the ribonuclease-albumin and the alpha-amylase-urease conjugate into their components with dithiothreitol. N-Succinimidyl 3-(2-pyridyldithio)propionate has been prepared in crystalline form, in which state (if protected against humidity) it is stable on storage at room temperature (23 degrees C).

Desmofibrin Formation and the Activity of the Fibrin Stabilizing Factor (FSF) during the Cleavage of Its SH Groups by Thrombin

1966 ◽  
Vol 16 (01/02) ◽  
pp. 051-060 ◽  
Author(s):  
K Buluk ◽  
J Olbromski ◽  
T Januszko ◽  
A Zuch
Keyword(s):  
Calcium Ions ◽  
Exchange Mechanism ◽  
Final Reaction ◽  
Sh Groups ◽  
Disulphide Bonds

SummaryIt was found that the activation of the FSF by thrombin in the presence of calcium ions takes place with a transitory increase of additional SH groups in the FSF.The activation of the FSF and the loss of its activity in the conversion of fibrin polymer to desmofibrin occurs simultaneously with the increase and decrease of additional SH groups.It is considered that in the transition of fibrin polymer to desmofibrin, the disulphide bonds exchange mechanism is involved, if not as a final reaction, at least as a phase in that mechanism.

THE RESULTS OF STUDYING THE EFFICIENCY OF DIATOMITE AT INTOXICATION OF ANIMALS WITH CADMIUM AND LEAD

2021 ◽  
Vol 1 (2) ◽  
pp. 214-222
Author(s):  
V.I. Dorozhkin ◽  
◽  
G.I. Pavlenko ◽  
N.S Pavlova ◽  
D.A. Drozdov ◽  
...  
Keyword(s):  
Heavy Metal ◽  
Body Weight ◽  
Blood Serum ◽  
Feed Additive ◽  
Protective Properties ◽  
Sh Groups ◽  
Lead And Cadmium ◽  
White Rats ◽  
Cadmium And Lead ◽  
Heavy Metal Intoxication

The combination of cadmium and lead in doses at the level of 10 MPC for feed caused in white rats a decrease in body weight and immunoglobulin content in blood serum, an increase in the summation threshold indicator, a decrease of the amount of protein in urine and SH-groups in blood serum, a significant increase in mass coefficients of the liver and kidneys. The use of diatomite as a means to reduce heavy metal intoxication slightly increased body weight. The use of means did not lead to normalization of the summation threshold indicator, did not significantly affect the content of SH-groups. In the group of animals treated with diatomite, the mass coefficients of the liver remained significantly higher than the control values. The obtained results indicate that diatomite did not show protective properties as a feed additive to reduce lead and cadmium intoxication.

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