THE ULTRASTRUCTURE OF HUMAN THYROGLOBULIN
1968 ◽
Vol 128
(5)
◽
pp. 1129-1136
◽
Keyword(s):
Thyroglobulin molecules purified in a single step procedure by gel filtration were studied in the electron microscope using the negative staining technique. The molecule had the shape of a flexible helix with two turns. Its length was about 220 A and the maximal diameter of the coiled part of the molecule was estimated to be 110 A. The pitch varied between 40 and 50 A. Thyroglobulin molecules dried in sodium tungstosilicate on a carbon film as for electron microscopy retained their hemagglutination-inhibiting activity and 19S sedimentation constant when redissolved in physiological buffer.
1968 ◽
Vol 127
(3)
◽
pp. 399-410
◽
Keyword(s):
1989 ◽
Vol 47
◽
pp. 444-445
1986 ◽
Vol 44
◽
pp. 696-697
◽
1990 ◽
Vol 48
(4)
◽
pp. 236-237
1978 ◽
Vol 36
(2)
◽
pp. 158-159
Keyword(s):
1983 ◽
Vol 41
◽
pp. 28-29
1978 ◽
Vol 36
(3)
◽
pp. 470-482
◽
1969 ◽
Vol 27
◽
pp. 12-13