scholarly journals Mechanism of SN2 Disulfide Bond Cleavage by Phosphorus Nucleophiles. Implications for Biochemical Disulfide Reducing Agents

2007 ◽  
Vol 72 (22) ◽  
pp. 8298-8307 ◽  
Author(s):  
Olga Dmitrenko ◽  
Colin Thorpe ◽  
Robert D. Bach
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
Reducing Agents

Alkali-modified soy proteins: Effect of salts and disulfide bond cleavage on adhesion and viscosity

1996 ◽  
Vol 73 (8) ◽  
pp. 1063-1066 ◽  
Author(s):  
U. Kalapathy ◽  
N. S. Hettiarachchy ◽  
D. Myers ◽  
K. C. Rhee
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
Soy Proteins

Facile Disulfide Bond Cleavage in Gaseous Peptide and Protein Cations by Ultraviolet Photodissociation at 157 nm

2005 ◽  
Vol 117 (39) ◽  
pp. 6557-6561 ◽  
Author(s):  
Y. M. Eva Fung ◽  
Frank Kjeldsen ◽  
Oleg A. Silivra ◽  
T. W. Dominic Chan ◽  
Roman A. Zubarev
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
Ultraviolet Photodissociation

Disulfide bond photochemistry: the effects of higher excited states and different molecular geometries on disulfide bond cleavage

2019 ◽  
Vol 21 (8) ◽  
pp. 4176-4183 ◽  
Author(s):  
Jun Cao ◽  
Dong-Chu Chen
Keyword(s):  
Excited State ◽  
Excited States ◽  
Disulfide Bond ◽  
Bond Cleavage ◽  
Trajectory Simulations ◽  
Higher Excited States

We have investigated the light-induced cleavage of disulfide bond using MS-CASPT2 based trajectory simulations and provided insights into the intrinsic excited state properties of disulfide molecules.

scholarly journals Effects of disulfide bond reducing agents on sperm chromatin structural integrity and developmental competence of in vitro matured oocytes after intracytoplasmic sperm injection in pigs

Reproduction ◽  
2009 ◽  
Vol 137 (4) ◽  
pp. 633-643 ◽  
Author(s):  
Wen-Min Cheng ◽  
Lei An ◽  
Zhong-Hong Wu ◽  
Yu-Bo Zhu ◽  
Jing-Hao Liu ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Intracytoplasmic Sperm Injection ◽  
Chemical Activation ◽  
Reducing Agents ◽  
Developmental Competence ◽  
Sperm Chromatin ◽  
Dna Integrity ◽  
Acridine Orange Staining ◽  
Sperm Dna

We recently reported that electrical activation followed by secondary chemical activation greatly enhanced the developmental competence ofin vitromatured porcine oocytes fertilized by intracytoplasmic sperm injection (ICSI). We hypothesized that sperm treatment with disulfide bond reducing agents will enhance the development competence of porcine embryos produced by this ICSI procedure. We examined the effects of glutathione (GSH), dithiothreitol (DTT), GSH or DTT in combination with heparin on sperm DNA structure, paternal chromosomal integrity, pronuclear formation, and developmental competence ofin vitromatured porcine oocytes after ICSI. Acridine orange staining and flow cytometry based sperm chromatin structure assay were used to determine sperm DNA integrity by calculating the cells outside the main population (COMP αT). No differences were observed in COMP αT values among GSH-treated and control groups. COMP αT values in GSH-treated groups were significantly lower than that in DTT-treated groups. Following ICSI, GSH treatments did not significantly alter paternal chromosomal integrity. Paternal chromosomal integrity in sperm treated with DTT plus or minus heparin was also the lowest among all groups. GSH-treated sperm yielded the highest rates of normal fertilization and blastocyst formation, which were significantly higher than that of control and DTT-treated groups. The majority of blastocysts derived from control and GSH-treated spermatozoa were diploid, whereas blastocysts derived from DTT-treated spermatozoa were haploid. In conclusion, sperm treatment with GSH enhanced the developmental capacity of porcine embryos produced by our optimized ICSI procedure.

Disulfide-Bond Cleavage and Formation in Proteins

Science ◽  
1965 ◽  
Vol 150 (3703) ◽  
pp. 1595-1598 ◽  
Author(s):  
O. Smithies
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage

Disulfide bond cleavage of human serum albumin and alterations of its secondary structure by cis-diamminedichloroplatinum(II)

1992 ◽  
Vol 85 (1-3) ◽  
pp. 39-44 ◽  
Author(s):  
Naoko Ohta ◽  
Toshihisa Yotsuyanagi ◽  
Danni Chen ◽  
Rikako Ono ◽  
Shigekazu Ito ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bond ◽  
Bond Cleavage

Effect of disulfide bond cleavage on the structure and conformation of glycinin

2009 ◽  
Vol 27 (4) ◽  
pp. 421-432 ◽  
Author(s):  
NAVIN KUMAR D. KELLA ◽  
WILLIAM E. BARBEAU ◽  
JOHN E. KINSELLA
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage

The Janus-faced role of external forces in mechanochemical disulfide bond cleavage

2013 ◽  
Vol 5 (8) ◽  
pp. 685-691 ◽  
Author(s):  
Przemyslaw Dopieralski ◽  
Jordi Ribas-Arino ◽  
Padmesh Anjukandi ◽  
Martin Krupicka ◽  
Janos Kiss ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Bond Cleavage ◽  
External Forces

Determination of —SH and —SS— groups in proteins. I. A reassessment of the use of methylmercuric iodide

1968 ◽  
Vol 46 (19) ◽  
pp. 3033-3040 ◽  
Author(s):  
W. F. Forbes ◽  
C. R. Hamlin
Keyword(s):  
Quantitative Determination ◽  
Disulfide Bond ◽  
Bond Cleavage ◽  
Reaction Times ◽  
High Reactivity ◽  
Insoluble Protein ◽  
Amperometric Titration ◽  
General Belief ◽  
Experimental Procedure

Amperometric titration with methylmercuric iodide was found to be unsatisfactory for the quantitative determination of —SH and —SS— values in several soluble proteins. It is concluded that the "high reactivity" of the mercurial has previously been overemphasized. Consistent values can, however, be obtained by permitting protein samples to react with an excess of the mercurial, for about 100 h, followed by the polarographic estimation of the remaining reagent. Contrary to general belief, this procedure was found to be more precise than amperometric titration, and, if appropriate precautions are taken, it is applicable to considerably smaller amounts (<0.5 μmole —SH or —SS—) of either soluble or insoluble protein. The necessary experimental procedure is described and results are reported for several proteins. For the compounds studied, methylmercuric iodide did not react at non-sulfhydryl sites, and did not additionally bind to the mercaptides formed; there was no indication of disulfide bond cleavage, despite the long reaction times used.

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