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Title: Studies in the molecular organisation of the nuclear envelope
Author: Richardson, Jonathan C. W.
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1979
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Immobilised lactoperoxidase has been developed as a probe of the molecular organisation of the nuclear envelope. In particular, it has been used to identify proteins of the nuclear pore complex (which is believed to be the principle site for nucleocytoplasmic transport of ribonucleoprotein) and to investigate the extent to which the nuclear membranes are differentiated from rough endoplasmic reticulum. The outer annulus of the nuclear pore complex is shown to comprise at least 14 polypeptides, only two of which (N1 and N2) are major components of the nuclear envelope as a whole. A third major component of the nuclear envelope (N3) is located in the fibrous meshwork that underlies and interconnects the pore complexes, and which represents the peripheral aspect of the nuclear matrix. The polypeptides of the nuclear envelope and rough endoplasmic reticulum are examined with respect to their distribution and organisation. It is firmly established, contrary to widely-held beliefs, that the nuclear membranes are a highly specialised membrane system quite distinct from the rough endoplasmic reticulum.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available