The Role of Disulfide Linkages in Desulfurization Chemistry: The Reactions of Benzenethiol on a Sulfur-Covered Mo(110) Surface

1994 ◽  
Vol 116 (18) ◽  
pp. 8328-8334 ◽  
Author(s):  
M. K. Weldon ◽  
M. E. Napier ◽  
Benjamin C. Wiegand ◽  
C. M. Friend ◽  
P. Uvdal
Keyword(s):  
Biochemistry ◽  
1993 ◽  
Vol 32 (43) ◽  
pp. 11704-11710 ◽  
Author(s):  
Katsumi Matsuzaki ◽  
Mitsuya Nakayama ◽  
Masaru Fukui ◽  
Akira Otaka ◽  
Susumu Funakoshi ◽  
...  

2017 ◽  
Vol 23 (5) ◽  
pp. 367-373 ◽  
Author(s):  
Danushka Arachchige ◽  
M. Margaret Harris ◽  
Zachary Coon ◽  
Jacob Carlsen ◽  
Justin M. Holub

1996 ◽  
Vol 74 (3) ◽  
pp. 391-401 ◽  
Author(s):  
Suresh C. Tyagi

To understand the role of thiol and oxidative mixed-disulfide exchange reaction in serpins, we analyzed the conformation of native and mixed-disulfide forms of α1-proteinase inhibitor (α1PI), α1-antichymotrypsin (α1-ACT), α2-antiplasmin (α2-AP), angiotensinogen, and ovalbumin. The conformation of native and oxidized mixed-disulfide serpins was measured by transverse urea gradient (TUG) gels. The results suggest that the acute phase proteins α1-PI and α1-ACT undergo conformational changes following oxidative mixed-disulfide formation and that α2-AP and angiotensinogen do not. The kinetics of disulfide formation was followed by measuring changes in absorbance at 412 nm resulting from Ellman's reaction of disulfide exchange. The rate of mixed-disulfide formation in albumin was 10-fold faster than in the serpin tested. The rate of disulfide exchange in α1-PI was 2-fold faster than that of α1-ACT. However, disulfide formation in α1-PI and α1-ACT was much slower than for any other serpin, e.g., α2-AP and angiotensinogen. We present evidence that α1-PI forms a dimer sensitive to thiol reduction, suggesting cysteinyl-mediated dimerization of α1-PI. The α1-PI also demonstrated two types of inter-protein disulfide linkages: one resulting in homodimer and other involving heterodimer formation. TUG–Western immunoblot methodology was developed to identify the conformational changes in serpins. We found that the conformational changes in serpins by mixed-disulfide formation are due to unfolding and not to decomposition or degradation in TUG gels. Using fluorescence measurements with isolated tryptic fragments of fluorescence-labelled elastase, we observed that the cysteinyl232 in α1-PI interacted with the cysteinyl168 of elastase in the proteinase–inhibitor complex. Our data suggests that serpin thiols may play an important role in forming a stable serpin–proteinase complex.Key words: serpin, extracellular matrix, proteinase, reduction, oxidation, inhibitor.


2017 ◽  
Vol 2017 ◽  
pp. 1-12 ◽  
Author(s):  
Barcley T. Pace ◽  
Andrew A. Lackner ◽  
Edith Porter ◽  
Bapi Pahar

Profound loss of CD4+T cells, progressive impairment of the immune system, inflammation, and sustained immune activation are the characteristics of human immunodeficiency virus-1 (HIV-1) infection. Innate immune responses respond immediately from the day of HIV infection, and a thorough understanding of the interaction between several innate immune cells and HIV-1 is essential to determine to what extent those cells play a crucial role in controlling HIV-1in vivo. Defensins, divided into the three subfamiliesα-,β-, andθ-defensins based on structure and disulfide linkages, comprise a critical component of the innate immune response and exhibit anti-HIV-1 activities and immunomodulatory capabilities. In humans, onlyα- andβ-defensins are expressed in various tissues and have broad impacts on HIV-1 transmission, replication, and disease progression.θ-defensins have been identified as functional peptides in Old World monkeys, but not in humans. Instead,θ-defensins exist only as pseudogenes in humans, chimpanzees, and gorillas. The use of the syntheticθ-defensin peptide “retrocyclin” as an antiviral therapy was shown to be promising, and further research into the development of defensin-based HIV-1 therapeutics is needed. This review focuses on the role of defensins in HIV-1 pathogenesis and highlights future research efforts that warrant investigation.


1989 ◽  
Vol 170 (6) ◽  
pp. 2051-2063 ◽  
Author(s):  
T L Wasmoen ◽  
D J McKean ◽  
K Benirschke ◽  
C B Coulam ◽  
G J Gleich

A protein immunochemically related to the eosinophil granule major basic protein (gMBP) is found in increased concentration in the plasma of pregnant women and has been localized to placental trophoblasts by immunofluorescence. Pregnancy MBP (pMBP) is indistinguishable from gMBP in its reactivity with polyclonal antisera and a panel of 14 mouse mAbs. We report the purification of pMBP from human placenta by: (a) affinity chromatography over mAb immobilized on Sepharose, (b) gel filtration in 6 M guanidine.HCl buffer, and (c) reversed-phase HPLC. Purified pMBP and gMBP are biochemically indistinguishable in that both: (a) bind to DNA, (b) polymerize and bind to carrier proteins via disulfide linkages, (c) have a molecular weight of 14,000, (d) have isoelectric points greater than 10.6, (e) comigrate in two-dimensional gels, (f) coelute during reversed-phase HPLC on C18 columns, (g) have identical peptide maps after three different digestions, and (h) have partial amino acid sequence identity. This physicochemical identity has important implications as to the role of pMBP in human placentation.


JAMA ◽  
1966 ◽  
Vol 195 (12) ◽  
pp. 1005-1009 ◽  
Author(s):  
D. J. Fernbach
Keyword(s):  

JAMA ◽  
1966 ◽  
Vol 195 (3) ◽  
pp. 167-172 ◽  
Author(s):  
T. E. Van Metre

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