scholarly journals Nuclear Clusters and Covalently Bound Nuclear Molecules

2002 ◽  
Vol 146 ◽  
pp. 169-178 ◽  
Author(s):  
Wolfram von Oertzen
Keyword(s):  
Nuclear Molecules ◽  
Nuclear Clusters ◽  
Covalently Bound

Clusters and covalently bound nuclear molecules

2003 ◽  
Vol 66 (9) ◽  
pp. 1591-1598 ◽  
Author(s):  
W. von Oertzen
Keyword(s):  
Nuclear Molecules ◽  
Covalently Bound

Nuclear clusters and nuclear molecules

2006 ◽  
Vol 432 (2) ◽  
pp. 43-113 ◽  
Author(s):  
W VONOERTZEN ◽  
M FREER ◽  
Y KANADAENYO
Keyword(s):  
Nuclear Molecules ◽  
Nuclear Clusters

scholarly journals QUARKS AND NEUTRON HALO NUCLEI, NUCLEAR CLUSTERS AND NUCLEAR MOLECULES

2001 ◽  
Vol 16 (12) ◽  
pp. 755-761 ◽  
Author(s):  
AFSAR ABBAS
Keyword(s):  
Ground State ◽  
Halo Nuclei ◽  
Neutron Halo ◽  
Comprehensive Understanding ◽  
Properties Of Nuclei ◽  
Ground State Properties ◽  
Nuclear Molecules ◽  
Nuclear Clusters ◽  
Nuclear Effects

It is shown that the hole in the centre of 3 H , 3 He and 4 He , the neutron halos in nuclei, the α- and other clustering effects in nuclei and the nuclear molecules all basically arise due to the same underlying effect. We shall show that all these ground state properties of nuclei are manifestations of quark effects. The role of triton clustering in very neutron rich nuclei is emphasized. All these require the concept of hidden colour states which arise from confinement ideas of QCD for the multi-quark systems. This provides a comprehensive understanding of diverse nuclear effects and makes unique predictions.

Adsorption of Fibrinogen and Fragment D of Fibrinogen onto the Insolubilized αChain of Fibrin

1979 ◽  
Vol 41 (04) ◽  
pp. 687-690
Author(s):  
F R Matthias
Keyword(s):  
Disulfide Bridges ◽  
Soluble Fibrin ◽  
Immobilized Proteins ◽  
Covalently Bound

SummaryAfter thrombin treatment insolubilized fibrinmonomer, which is obtained from insolubilized fibrinogen covalently bound to agarose, adsorbs soluble fibrin and its derivatives from solutions. The immobilized proteins are attached to the agarose by the ‘A’ αchain. After reduction of the disulfide bridges the β and γchains can be removed from the agarose.After thrombin treatment the immobilized αchain adsorbs fibrinogen and fragment D. To some extent the β and γchain do not seem necessary for the adsorption. The amount adsorbed increases, when thrombin treatment of the insolubilized protein follows the reduction process.This may indicate that the fibrinopeptides ‘A’ of the insolubilized αchain are better accessible after the removal of the β and γchains.

INTERFERENCE BY SERUM PROTEINS WITH LH RADIOIMMUNOASSAY USING IMMUNOSORBENT

1973 ◽  
Vol 72 (2) ◽  
pp. 235-242 ◽  
Author(s):  
A. M. Reuter ◽  
J. C. Hendrick ◽  
J. Sulon ◽  
P. Franchimont
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
High Molecular Weight ◽  
Serum Proteins ◽  
Void Volume ◽  
High Molecular Weight Proteins ◽  
Serum Fractionation ◽  
Covalently Bound

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.

Sign in / Sign up

Export Citation Format

Share Document