Charge control in the formation of complexes of phenol with unsaturated compounds containing organometallic substituents from group IV

1994 ◽  
Vol 43 (6) ◽  
pp. 976-982
Author(s):  
A. N. Egorochkin ◽  
S. E. Skobeleva ◽  
E. T. Bogoradovsky ◽  
T. P. Zubova
Keyword(s):  
Group Iv ◽  
Charge Control ◽  
Unsaturated Compounds ◽  
Formation Of Complexes

Luminescence from individual dislocations in II-VI and III-V semiconductors

1991 ◽  
Vol 49 ◽  
pp. 834-835
Author(s):  
J W Steeds
Keyword(s):  
Group Iv ◽  
Luminescence Properties ◽  
Carrier Recombination ◽  
Transmission Electron ◽  
Wide Range ◽  
Basic Physics ◽  
Semiconducting Compounds ◽  
Diamond Group ◽  
Non Destructive ◽  
Technological Significance

There is a wide range of experimental results related to dislocations in diamond, group IV, II-VI, III-V semiconducting compounds, but few of these come from isolated, well-characterized individual dislocations. We are here concerned with only those results obtained in a transmission electron microscope so that the dislocations responsible were individually imaged. The luminescence properties of the dislocations were studied by cathodoluminescence performed at low temperatures (~30K) achieved by liquid helium cooling. Both spectra and monochromatic cathodoluminescence images have been obtained, in some cases as a function of temperature.There are two aspects of this work. One is mainly of technological significance. By understanding the luminescence properties of dislocations in epitaxial structures, future non-destructive evaluation will be enhanced. The second aim is to arrive at a good detailed understanding of the basic physics associated with carrier recombination near dislocations as revealed by local luminescence properties.

ISOMER-SHIFT SYSTEMATICS OF 57Co IMPLANTED IN GROUP IV SEMICONDUCTORS

1976 ◽  
Vol 37 (C6) ◽  
pp. C6-893-C6-896 ◽  
Author(s):  
G. WEYER ◽  
G. GREBE ◽  
A. KETTSCHAU ◽  
B. I. DEUTCH ◽  
A. NYLANDSTED LARSEN ◽  
...  
Keyword(s):  
Isomer Shift ◽  
Group Iv ◽  
Group Iv Semiconductors

Mutations which Introduce Free Cysteine Residues in the Gla-Domain of Vitamin K Dependent Proteins Result in the Formation of Complexes with α1-Microglobulin

1996 ◽  
Vol 75 (01) ◽  
pp. 070-075 ◽  
Author(s):  
E G C Wojcik ◽  
P Simioni ◽  
M v d Berg ◽  
A Girolami ◽  
R M Bertina
Keyword(s):  
Vitamin K ◽  
Protein C ◽  
Cysteine Residue ◽  
Factor Ix ◽  
Disulphide Bond ◽  
Clotting Factors ◽  
High Molecular Weight Complex ◽  
Low Concentrations ◽  
Gla Domain ◽  
Formation Of Complexes

SummaryWe have previously described a genetic factor IX variant (Cys18→Arg) for which we demonstrated that it had formed a heterodimer with armicroglobulin through formation of a disulphide bond with the remaining free cysteine residue of the disrupted disulphide bond in the Gla-domain of factor IX. Recently, we observed a similar high molecular weight complex for a genetic protein C variant (Arg-1→Cys). Both the factor IX and the protein C variants have a defect in the calcium induced conformation. In this study we show that the aminoterminus of this protein C variant is prolonged with one amino acid, cysteine. This protein C variant, as well as protein C variants with Arg9→Cys and Ser12→Cys mutations which also carry a free cysteine residue, are shown to be present in plasma as a complex with α1-microglobulin. A prothrombin variant with a Tyr44→Cys mutation, had not formed such a complex. Furthermore, complexes between normal vitamin K-dependent clotting factors and α1-microglobulin were shown to be present in plasma at low concentrations. The data suggest that the presence of an unpaired cysteine residue in the propeptide or the N-terminal half of the Gla-domain has strongly promoted the formation of a complex with α1-microglobulin in the variants.

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