British journal of anaesthesia, 53(6), 577-584 (1981-06-01)
Xenopus laevis tadpoles were produced from wild-caught, laboratory-reared toads. Separate sets were fed on diets of (1) liver powder; (2) nettle powder; (3) aminosol and Intralipid. The tadpoles were reared for 3 weeks at 22 degrees C and then three
Labeling of hydrophobic polypeptides from the chick lens membrane.
The Biochemical journal, 236(2), 389-395 (1986-06-01)
Opsin labelled with photoactivated 1-azido-4-[125I]iodobenzene was proteolysed in situ with Staphylococcus aureus V8 proteinase to yield two radioactive membrane-bound fragments. These were separated, cleaved with CNBr and the resultant peptides sequenced in order to locate the radiolabelled residues. In the
The Biochemical journal, 234(2), 413-420 (1986-03-01)
The hydrophobic photosensitive probe 1-azido-4-[125I]iodobenzene (AIB) partitioned preferentially into photoreceptor disc membranes and, upon u.v. irradiation, became covalently bound to opsin and phospholipid. The labelling of both protein and phospholipid was linearly related to AIB concentration. The amount of probe
The Biochemical journal, 187(3), 719-725 (1980-06-01)
To investigate the intramembranous domains of the major band-3 polypeptide, human erythrocyte membranes were labelled with 1-azido-4-[125I]iodobenzene. The anion-exchange protein has been isolated by a new procedure that decreases possible contamination by other integral membrane proteins of similar molecular weight.
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