The polypeptides of rat liver nuclear envelope. I. Examination by nuclear pore complex polypeptides by solid-state lactoperoxidase labelling.

Abstract:

:Purified nuclei retaining a high degree of ultrastructural integrity were isolated by conventional centrifugation techniques. The cytoplasmic surface of these nuclei was iodinated using lactoperoxidase immobilized onto giant Sepharose beads; thus the outer nuclear membrane and the cytoplasmic surface of nuclear pore complexes were selectively labelled. Pore complexes in association with a fibrous lamina were isolated from these nuclei by removal of the nucleoplasm and extraction with Triton X-100. The chemical composition of the pore-lamina fraction was 93.6% protein, 6% RNA, 0.4% phospholipid. The labelling suggests that major polypeptides N1 (70 000) and N2 (67 000) and more than 10 other more minor polypeptides, ranging from 33 000 to 200 000 mol. wt, as being components of the nuclear pore complex. Polypeptide N3 (58 000) is shown to be present only on the nucleoplasmic face of nuclear envelopes, probably in the fibrous lamina.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Richardson JC,Maddy AH

subject

Has Abstract

pub_date

1980-06-01 00:00:00

pages

253-67

eissn

0021-9533

issn

1477-9137

journal_volume

43

pub_type

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