Complex Formation Between Chymotrypsin and Ethyl Cellulose as a Means to Solubilize the Enzyme in Active Form in Toluene

Biocatalysis ◽  
1992 ◽  
Vol 6 (4) ◽  
pp. 291-305 ◽  
Author(s):  
Marina Otamiri ◽  
Patrick Adlercreutz ◽  
Bo Mattiasson
Keyword(s):  
Complex Formation ◽  
Ethyl Cellulose ◽  
Active Form

scholarly journals Peptide-chain initiation in duodenal mucosa of rachitic chicks after 1α-,25-dihydroxycholecalciferol administration

1984 ◽  
Vol 219 (1) ◽  
pp. 99-106 ◽  
Author(s):  
G Mezzetti ◽  
M Moruzzi ◽  
B Barbiroli
Keyword(s):  
Complex Formation ◽  
Gradient Centrifugation ◽  
Active Form ◽  
Ribosomal Subunit ◽  
Sucrose Density Gradient ◽  
Duodenal Mucosa ◽  
Binding Activity ◽  
Initiation Factor ◽  
Experimental Conditions ◽  
Sucrose Density Gradient Centrifugation

The post-ribosomal fraction of chick duodenal mucosa contains Met-tRNAMetf-binding protein(s) that behaves like the eukaryotic initiation factor (eIF-2) in protein synthesis. The binding activity of cytosol protein can be measured by retention of the radioactive complex formed on a nitrocellulose membrane. Complex-formation requires Met-tRNAMetf and GTP or guanosine [beta, gamma-methylene] triphosphate, and is inhibited by aurintricarboxylic acid. The ternary initiation complex thus formed can bind to ribosomal particles from chick intestine. By sucrose-density-gradient centrifugation, [35S]Met-tRNAMetf was found to bind exclusively to 40S and not to 60S ribosomal subunit particles. In the duodenal mucosa of rachitic chicks the ability of the cytosol proteins to promote the binding of Met-tRNAMetf to ribosomal particles via ternary-complex formation is detectably increased by 3 h after injection of 1 alpha,25-dihydroxycholecalciferol, the active form of vitamin D. Cholecalciferol and ergocalciferol under the same experimental conditions failed to stimulate Met-tRNAMetf-binding activity.

scholarly journals Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex

2016 ◽  
Vol 198 (7) ◽  
pp. 1160-1170 ◽  
Author(s):  
Begoña Stevenson ◽  
Elizabeth E. Wyckoff ◽  
Shelley M. Payne
Keyword(s):  
Complex Formation ◽  
Vibrio Cholerae ◽  
Ferrous Iron ◽  
Iron Transport ◽  
Active Form ◽  
Integral Membrane Protein ◽  
Content Type ◽  
Membrane Complex ◽  
Ferrous Iron Transport

ABSTRACTFeo is the major ferrous iron transport system in prokaryotes. Despite having been discovered over 25 years ago and found to be widely distributed among bacteria, Feo is poorly understood, as its structure and mechanism of iron transport have not been determined. Thefeooperon inVibrio choleraeis made up of three genes, encoding the FeoA, FeoB, and FeoC proteins, which are all required for Feo system function. FeoA and FeoC are both small cytoplasmic proteins, and their function remains unclear. FeoB, which is thought to function as a ferrous iron permease, is a large integral membrane protein made up of an N-terminal GTPase domain and a C-terminal membrane-spanning region. To date, structural studies of FeoB have been carried out using a truncated form of the protein encompassing only the N-terminal GTPase region. In this report, we show that full-length FeoB forms higher-order complexes when cross-linkedin vivoinV. cholerae. Our analysis of these complexes revealed that FeoB can simultaneously associate with both FeoA and FeoC to form a large complex, an observation that has not been reported previously. We demonstrate that interactions between FeoB and FeoA, but not between FeoB and FeoC, are required for complex formation. Additionally, we identify amino acid residues in the GTPase region of FeoB that are required for function of the Feo system and for complex formation. These observations suggest that this large Feo complex may be the active form of Feo that is used for ferrous iron transport.IMPORTANCEThe Feo system is the major route for ferrous iron transport in bacteria. In this work, theVibrio choleraeFeo proteins, FeoA, FeoB, and FeoC, are shown to interact to form a large inner membrane complexin vivo. This is the first report showing an interaction among all three Feo proteins. It is also determined that FeoA, but not FeoC, is required for Feo complex assembly.

Dupuytren's Contracture and Microvessels

1981 ◽  
Vol 39 ◽  
pp. 470-471
Author(s):  
C. W. Klscher ◽  
D. Speer
Keyword(s):  
Hypertrophic Scar ◽  
Active Form ◽  
Scar Tissue ◽  
Vascular Supply ◽  
Fiber Bundles ◽  
Dupuytren’S Contracture ◽  
Palmar Fascia ◽  
Immune Disease ◽  
Dupuytren's Contracture ◽  
Longitudinal Fiber

Dupuytren's Contracture is a nodular proliferation of the longitudinal fiber bundles of palmar fascia with its attendant contraction. The factors attributed to its etiology have included trauma, diabetes, alcoholism, arthritis, and auto-immune disease. The tissue has been observed by electron microscopy and found to contain myofibroblasts.Dupuytren's Contracture constitutes a scar, and as such, excessive collagen can be observed, along with an active form of fibroblast.Previous studies of the hypertrophic scar have led us to propose that integral in the initiation and sustenance of scar tissue is a profusion of microvascular regeneration, much of which becomes and remains occluded producing a hypoxia which stimulates fibroblast synthesis. Thus, when considering a study of Dupuytren's Contracture, we predicted finding occluded microvessels at or near the fascial scarring focus.Three cases of Dupuytren's Contracture yielded similar specimens, which were fixed in Karnovskys fluid for 2 to 20 days. Upon removal of the contracture bands care was taken to include the contiguous fatty and areolar tissue which contain the vascular supply and to identify the junctional area between old and new fascia.

Integrated morphometrical and electron energy loss image analysis in cytochemistry

1989 ◽  
Vol 47 ◽  
pp. 402-403
Author(s):  
W.C. de Bruijn ◽  
A.A.W. de Jong ◽  
C.W.J. Sorber
Keyword(s):  
Image Analysis ◽  
Acid Phosphatase ◽  
Chemical Analysis ◽  
Active Form ◽  
List Type ◽  
Type Number ◽  
Enzyme Cytochemistry ◽  
Related Data ◽  
Endogenous Peroxidase ◽  
Electron Energy Loss

One aspect of enzyme cytochemistry is, whether all macrophage lysosomal hydrolytical enzymes are present in an active form, or are activated upon stimulation. Integrated morphometrical and chemical analysis has been chosen as a tool to illucidate that cytochemical problem. Mouse peritoneal resident macrophages have been used as a model for this complicated integration of morphometrical and element-related data. Only aldehyde-fixed cells were treated with three cytochemical reactions to detect different enzyme activities within one cell (for details see [1,2]). The enzyme-related precipitates anticipated to be differentiated, were:(1).lysosomal barium and sulphur from aryl sulphatase activity,(2).lysosomal cerium and phosphate from acid phosphatase activity and(3).platinum/di-amino-benzidine( D A B) complex from endogenous peroxidase activity.

Comparative Labelling and Biokinetic Studies of 99mTc-EDTA(Sn) and 99mTc-DTPA(Sn)

1977 ◽  
Vol 16 (01) ◽  
pp. 30-35 ◽  
Author(s):  
N. Agha ◽  
R. B. R. Persson
Keyword(s):  
Complex Formation ◽  
Significant Influence ◽  
Room Temperature ◽  
Ph Value ◽  
Maximum Activity ◽  
Reduction Step ◽  
Labelling Yield ◽  
Different Temperatures ◽  
Kinetics Of

SummaryGelchromatography column scanning has been used to study the fractions of 99mTc-pertechnetate, 99mTcchelate and reduced hydrolyzed 99mTc in preparations of 99mTc-EDTA(Sn) and 99mTc-DTPA(Sn). The labelling yield of 99mTc-EDTA(Sn) chelate was as high as 90—95% when 100 μmol EDTA · H4 and 0.5 (Amol SnCl2 was incubated with 10 ml 99mTceluate for 30—60 min at room temperature. The study of the influence of the pH-value on the fraction of 99mTc-EDTA shows that pH 2.8—2.9 gave the best labelling yield. In a comparative study of the labelling kinetics of 99mTc-EDTA(Sn) and 99mTc- DTPA(Sn) at different temperatures (7, 22 and 37°C), no significant influence on the reduction step was found. The rate constant for complex formation, however, increased more rapidly with increased temperature for 99mTc-DTPA(Sn). At room temperature only a few minutes was required to achieve a high labelling yield with 99mTc-DTPA(Sn) whereas about 60 min was required for 99mTc-EDTA(Sn). Comparative biokinetic studies in rabbits showed that the maximum activity in kidneys is achieved after 12 min with 99mTc-EDTA(Sn) but already after 6 min with 99mTc-DTPA(Sn). The long-term disappearance of 99mTc-DTPA(Sn) from the kidneys is about five times faster than that for 99mTc-EDTA(Sn).

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