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• W2158744079 abstract "SUMMARYHaemoglobin from an amphibian, Bufo melanostictus, was studied by electron microscopy after metal shadowing and after negative staining with uranyl acetate. The effect of the electron stain on the protein was investigated by spectrophotometry. The sample was also characterized by alkali denaturation and sedimentation analysis. The results were compared to those of adult human haemoglobin.Spectrophotometry of the sample showed characteristics similar to those of normal oxyhaemoglobin. The protein, like human adult haemoglobin, was found to be completely alkali-labile. Ultracentrifugation of a freshly prepared sample showed a single symmetrical peak, an indication for the presence of a homogeneous component. The S020,W value (5.1) was found to be markedly higher than that of adult human haemoglobin. With storage, however, the peak became asymmetrical suggesting the formation of a limited amount of a heavier component.The electron micrographs of the shadowed preparations revealed a characteristic shape and ultrastructure of the protein molecules and their average height was found to be 5.5 nm. The micrographs of the negatively stained samples showed many particles with a substructure similar to that of the shadowed molecules and a mean dimension of 6.1 nm, a number of dimers of average length 6.0 nm and overall width 3.6 nm, and many globules of average diameter 3.6 nm. These were interpreted as whole, half and quarter haemoglobin molecules, respectively. Both techniques revealed at the most four subunits in a molecule. The structure of the subunits and their arrangement in the molecule were found to be essentially similar to those of normal human adult haemoglobin, and could be interpreted in terms of the Perutz model. Spectrophotometry of the mixture of the protein and uranyl acetate showed that the protein becomes denatured with time and that the denaturation is due to the low pH (4.3) of the stain. Nevertheless, this study showed that by keeping the staining time very short, it is possible to obtain acceptable electron micrographs of small multi-unit protein molecules such as haemoglobin." @default.
• W2158744079 created "2016-06-24" @default.
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• W2158744079 date "1971-06-01" @default.
• W2158744079 modified "2023-09-27" @default.
• W2158744079 title "Studies on haemoglobin from the Indian toad, Bufo melanostictus, by electron microscopy" @default.
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• W2158744079 doi "https://doi.org/10.1111/j.1365-2818.1971.tb02282.x" @default.
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