Monoclonal antibody-based immunoaffinity chromatography for purifying corn and squash NADH: nitrate reductases. Evidence for an interchain disulfide bond in nitrate reductase

1989 ◽  
Vol 13 (2) ◽  
pp. 233-246 ◽  
Author(s):  
Gregory E. Hyde ◽  
Julie A. Wilberding ◽  
Annette L. Meyer ◽  
Ellen R. Campbell ◽  
Wilbur H. Campbell
Keyword(s):  
Monoclonal Antibody ◽  
Nitrate Reductase ◽  
Disulfide Bond ◽  
Immunoaffinity Chromatography ◽  
Interchain Disulfide Bond ◽  
Nitrate Reductases

scholarly journals Effects of an Interchain Disulfide Bond on Tropomyosin Structure: A Molecular Dynamics Study

2018 ◽  
Vol 19 (11) ◽  
pp. 3376 ◽  
Author(s):  
Natalia A. Koubassova ◽  
Sergey Y. Bershitsky ◽  
Andrey K. Tsaturyan
Keyword(s):  
Heart Failure ◽  
Molecular Dynamics ◽  
Disulfide Bond ◽  
Coiled Coil ◽  
Middle Part ◽  
Actin Binding ◽  
Cross Linking ◽  
Interchain Disulfide Bond ◽  
Structural And Functional Properties ◽  
The Cross

Tropomyosin (Tpm) is a coiled-coil actin-binding dimer protein that participates in the regulation of muscle contraction. Both Tpm chains contain Cys190 residues which are normally in the reduced state, but form an interchain disulfide bond in failing heart. Changes in structural and functional properties of Tpm and its complexes with actin upon disulfide cross-linking were studied using various experimental methods. To understand the molecular mechanism underlying these changes and to reveal the possible mechanism of the involvement of the cross-linking in heart failure, molecular dynamics (MD) simulations of the middle part of Tpm were performed in cross-linked and reduced states. The cross-linking increased bending stiffness of Tpm assessed from MD trajectories at 27 °C in agreement with previous experimental observations. However, at 40 °C, the cross-linking caused a decrease in Tpm stiffness and a significant reduction in the number of main chain hydrogen bonds in the vicinity of residues 133 and 134. These data are in line with observations showing enhanced thermal unfolding of the least stable part of Tpm at 30–40 °C and accelerated trypsin cleavage at residue 133 at 40 °C (but not at 27 °C) upon cross-linking. These results allow us to speculate about the possible mechanism of involvement of Tpm cross-linking to heart failure pathogenesis.

scholarly journals A Relaxed Specificity in Interchain Disulfide Bond Formation Characterizes the Assembly of a Low-Molecular-Weight Glutenin Subunit in the Endoplasmic Reticulum

2008 ◽  
Vol 149 (1) ◽  
pp. 412-423 ◽  
Author(s):  
Alessio Lombardi ◽  
Alessandra Barbante ◽  
Pietro Della Cristina ◽  
Daniele Rosiello ◽  
Chiara Lara Castellazzi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Endoplasmic Reticulum ◽  
Disulfide Bond ◽  
Bond Formation ◽  
Glutenin Subunit ◽  
Low Molecular Weight ◽  
Disulfide Bond Formation ◽  
Interchain Disulfide Bond

scholarly journals Determination of Domoic Acid in Japanese Mussels by Enzyme Immunoassay

2000 ◽  
Vol 83 (6) ◽  
pp. 1384-1386 ◽  
Author(s):  
Kentaro Kawatsu ◽  
Yonekazu Hamano ◽  
Tamao Noguchi
Keyword(s):  
Monoclonal Antibody ◽  
Enzyme Immunoassay ◽  
Domoic Acid ◽  
Immunoaffinity Chromatography ◽  
Shellfish Poisoning ◽  
Mussel Tissue ◽  
Blue Mussels ◽  
Amnesic Shellfish Poisoning ◽  
Low Concentrations

Abstract Ten samples of commercial blue mussels (Mytilus edulis) from Japan were analyzed for domoic acid by an indirect competitive enzyme immunoassay (idc–EIA) based on an anti-domoic acid monoclonal antibody. Domoic acid was found in all samples at low concentrations (0.11–1.81 ng/g mussel tissue). The presence of domoic acid was confirmed by liquid chromatography coupled with immunoaffinity chromatography using an anti-domoic acid monoclonal antibody as ligand. To our knowledge, this is the first reported detection of domoic acid, a causative agent of amnesic shellfish poisoning, in Japanese mussels.

Immunization of merino ewes with a synthetic inhibin peptide or with preparations obtained from bovine and porcine follicular fluids by immunoaffinity chromatography result in different effects on ovulation rate and on plasma gonadotrophin concentrations

1991 ◽  
Vol 3 (6) ◽  
pp. 659 ◽  
Author(s):  
T O'Shea ◽  
CM Andrews ◽  
BM Bindon ◽  
MA Hillard ◽  
K Miyamoto ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Synthetic Peptide ◽  
Amino Acid Sequence Identity ◽  
Immunoaffinity Chromatography ◽  
Ovulation Rate ◽  
Alpha Subunit ◽  
Ovarian Activity ◽  
Amino Terminal ◽  
Sequence Identity ◽  
Follicular Fluids

Ewes were immunized with either a synthetic peptide (peptide 1-32) that has an amino acid sequence identity with the first 32 amino acids at the amino terminal of the alpha-subunit of porcine inhibin, or with bovine or porcine monoclonal antibody purified inhibin (bMPI and pMPI respectively), obtained by immunochromatography from follicular fluids. The peptide 1-32 was conjugated to albumin before use. Peptide 1-32 and bMPI increased ovulation rate and number of follicles (greater than or equal to 5 mm diameter). Although bMPI increased plasma FSH concentration the peptide did not. pMPI had no effect on ovarian activity but markedly elevated both plasma FSH and LH concentrations. The plasma LH concentration was lowered in ewes immunized with peptide 1-32. It appears, therefore, that ovulation rate can be increased following increased plasma FSH concentrations at luteolysis or in the absence of such an increase. Conversely, greatly increased plasma gonadotrophin concentrations at luteolysis (pMPI) were not followed by an increase in ovulation rate. Antibodies in the plasma of ewes immunized with peptide 1-32 and bMPI bound to iodinated synthetic human inhibin alpha-chain 6-30 peptide. The results suggest that ovulation rate is at least partly determined by intraovarian factors.

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